Anti-TCR antibody molecules and uses thereof

Abstract

The disclosure provides antibody molecules that bind to TCR Vβ regions and multispecific molecules comprising said antibody molecules. Additionally, disclosed are nucleic acids encoding the same, meth

Description

Current molecules designed to redirect T cells to promote tumor cell lysis for cancer immunotherapy typically target the CD3 epsilon (CD3e) subunit of the T cell receptor (TCR). However, there are limitations to this approach. Previous studies have shown that, e.g., low doses of anti-CD3e monoclonal antibody (mAb) can cause T cell dysfunction and exert immunosuppressive effects. In addition, anti-CD3e mAbs bind to all T cells and thus activate a large number of T cells. Such non-physiological massive activation of T cells by these anti-CD3e mAbs can result in the production of proinflammatory cytokines such as IFN-gamma, IL-1-beta, IL-6, IL-10 and TNF-alpha, causing a “cytokine storm” known as the cytokine release syndrome (CRS), which is also associated with neurotoxicity (NT). Thus, it might be advantageous to develop antibodies that avoid or reduce CRS and / or NT. SUMMARY OF THE INVENTION Disclosed herein are, inter alia, antibody molecules directed to the variable chain of the beta subunit of TCR (TCRpV) which bind and, e.g., activate or expand, T cells, e.g., a subset of T cells (“anti-TCRpV antibody molecules”). In some embodiments, the anti-TCRpV antibody molecules disclosed herein result in a cytokine profile, e.g., a cytokine secretion profile, that differs from that of a T cell engager that binds to a receptor or molecule other than a TCRPV region (“a non-TCRpV-binding T cell engager”). In some embodiments, the anti-TCRpV antibody molecules disclosed herein result in lesser, minimal, or no production of cytokines associated with cytokine release syndrome (CRS), e.g., IL-6, IL-lbeta, IL-10 and TNF alpha; and enhanced and / or delayed production of IL-2 and IFN-gamma. In some embodiments, the anti-TCRpV antibodies disclosed herein result in expansion of an immune cell, e.g., a T cell, a tumor infiltrating lymphocyte (TIL), an NK cell, or other immune cells (e.g., as described herein). Also provided herein are methods of making said anti-TCRpV antibody molecules, and methods of using said anti-TCRpV antibody molecules including, methods of using an anti-TCRPV antibody molecule for expanding an immune cell or an immune cell population, and method of using an anti-TCRpV antibody molecule for treating cancer, including the use as combination therapy with TIL and immune checkpoint therapeutics. This disclosure further provides multispecific molecules, e.g., bispecific molecules, comprising said anti-TCRpV antibody molecules. In some embodiments, compositions comprising anti-TCRpV antibody molecules of the present disclosure, can be used, e.g., to activate and / or redirect T cells to promote tumor cell lysis for cancer immunotherapy. In some embodiments, compositions comprising anti-TCRpV antibody molecules as disclosed herein limit the unwanted side-effects of CRS and / or NT, e.g., CRS and / or NT associated with anti-CD3e targeting. In some embodiments, the anti-TCRpV antibody molecules disclosed herein result in lesser, minimal, or no production of cytokines associated with cytokine release syndrome (CRS), e.g., IL-6, IL-lbeta, IL-10 and TNF alpha; and enhanced and / or delayed production of IL-2 and IFN-gamma, compared with an anti-CD3 antibody molecule (e.g., a low affinity anti-CD3 antibody molecule). In some embodiments, administration of the anti-TCRpV antibody molecules disclosed herein in a subject results in reduced cytokine release syndrome (CRS) (e.g., lesser duration of CRS or no CRS), a reduced severity of CRS (e.g., absence of severe CRS, e.g., CRS grade 4 or 5), reduced neurotoxicity (NT), or a reduced severity of NT, compared with similar administration of an anti-CD3 antibody molecule (e.g., a low affinity anti-CD3 antibody molecule). Accordingly, provided herein are, anti-TCRpV antibody molecules, multispecific or multifunctional molecules (e.g., multispecific or multifunctional antibody molecules) (also referred to herein as a “composition”) that comprise anti-TCRpV antibody molecules, nucleic acids encoding the same, methods of producing the aforesaid molecules, pharmaceutical compositions comprising aforesaid molecules, and methods of treating a disease or disorder, e.g., cancer, using the aforesaid molecules. The antibody molecules and pharmaceutical compositions disclosed herein can be used (alone or in combination with other agents or therapeutic modalities) to treat, prevent and / or diagnose disorders and conditions, e.g., cancer, e.g., as described herein. In one aspect, the disclosure provides an antibody molecule, e.g., a non-murine, e.g., a human-like (e.g., a human, or humanized antibody molecule), which binds, e.g., specifically binds, to a T cell receptor beta variable (TCRPV) region. In some embodiments, the anti-TCRBV antibody molecule comprises an antigen binding domain of an antibody disclosed in any of Tables 1-2, or 10-13, or a sequence with at least 85%, 90%, 95%, 96%, 97%, 98%, or 99% identity thereto. In some embodiments, the anti-TCRBV antibody molecule comprises a leader sequence comprising the amino acid sequence of SEQ ID NO: 3288. In some embodiments, the anti-TCRBV antibody molecule does not comprise a leader sequence comprising the amino acid sequence of SEQ ID NO: 3288. In some embodiments, binding of the anti-TCRpV antibody molecule to a TCRPV region results in a cytokine profile, e.g., a cytokine secretion profile, (e.g., comprising one or more cytokines and / or one or more chemokines), that differs from that of a T cell engager that binds to a receptor or molecule other than a TCRPV region (“a non-TCRpV-binding T cell engager”). In some embodiments, the cytokine profile, e.g., cytokine secretion profile, comprises one, two, three, four, five, six, seven, or all of the following: (i) increased level, e.g., expression level, and / or activity of IL-2; (ii) reduced level, e.g., expression level, and / or activity of IL-Ip; (iii) reduced level, e.g., expression level, and / or activity of IL-6; (iv) reduced level, e.g., expression level, and / or activity of TNFa; (v) reduced level, e.g., expression level, and / or activity of IL-10; (vi) a delay, e.g., at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 or more hours delay, in increased level, e.g., expression level, and / or activity of IL-2; (vii) a delay, e.g., at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 hours delay, in increased level, e.g., expression level, and / or activity of IFN-gamma; or (viii) increased level, e.g., expression level, and / or activity of IL-15, e.g., wherein (i)-(viii) are relative to the cytokine profile, e.g., cytokine secretion profile, of the non-TCRpV-binding T cell engager. In some embodiments, binding of the anti-TCRBV antibody to a TCRpV region results in reduced cytokine storm, e.g., reduced cytokine release syndrome (CRS) and / or neurotoxicity (NT), as measured by an assay of Example 3, e.g., relative to the cytokine storm induced by the non-TCRpV-binding T cell engager. In some embodiments, binding of the anti-TCRBV antibody to a TCRPV region results in one, two, three or all of: (ix) reduced T cell proliferation kinetics; (x) cell killing, e.g., target cell killing, e.g. cancer cell killing, e.g., as measured by an assay of Example 4; (xi) increased Natural Killer (NK) cell proliferation, e.g., expansion; or (xii) expansion, e.g., at least about 1.1-10 fold expansion (e.g., at least about 1.1, 1.2, 1.3, 1.4, 1.5, 2, 3, 4, 5, 6, 7, 8, 9, or 10 fold expansion), of a population of T cells having a memory-like phenotype, e.g., as described herein, e.g., wherein (ix)-(xii) are relative to the non-TCRpV-binding T cell engager. 3 In some embodiments, an anti-TCRpV antibody molecule disclosed herein recognizes (e.g., binds to), a structurally conserved domain on the TCRPV protein (e.g., as denoted by the circled area in FIG. 24A). In some embodiments, an anti-TCRVP antibody disclosed herein comprises an Fc region, e.g., as described herein. In some embodiments, the Fc region is a wildtype Fc region, e.g., a wildtype human Fc region. In some embodiments, the Fc region comprises a variant, e.g., an Fc region comprising an addition, substitution, or deletion of at least one amino acid residue in the Fc region which results in, e.g., reduced affinity for and / or binding to, at least one Fc receptor. In some embodiments, the reduced affinity is compared to an otherwise similar antibody with a wildtype Fc region. In some embodiments, an anti-TCRVP antibody comprising a variant Fc region has one or more of the following properties: (1) reduced effector function (e.g., reduced ADCC, ADCP and / or CDC); (2) reduced binding to one or more Fc receptors; and / or (3) reduced binding to Clq complement. In some embodiments, the reduction in any one, or all of properties (1)-(3) is compared to an otherwise similar antibody with a wildtype Fc region. In some embodiments, an anti-TCRVp antibody comprising a variant Fc region has reduced affinity to a human Fc receptor, e g., FcyR I, FcyR II and / or FcyR III. In some embodiments, the anti-TCRVp antibody comprising a variant Fc region comprises a human IgGl region or a human IgG4 region. In some embodiments, an anti-TCRVp antibody disclosed herein comprises any one or all, or any combination of Fc region variants, e.g., mutations, disclosed in Table 21. In some embodiments, an anti-TCRVp antibody disclosed herein comprise an Asn297Ala (N297A) mutation. In some embodiments, an anti-TCRVp antibody disclosed herein comprise a Leu234Ala / Leu235Ala (LALA) mutation. In some embodiments, an anti-TCRpV antibody molecule disclosed herein does not recognize, e.g., bind to, an interface of a TCRpV :TCRalpha complex. In some embodiments, an anti-TCRpV antibody molecule disclosed herein does not recognize, e.g., bind to, a constant region of a TCRPV protein. An exemplary antibody that binds to a constant region of a TCRBV region is JOVI. 1 as described in Viney et al., (Hybridoma. 1992 Dec;l 1(6):701-13). In some embodiments, an anti-TCRpV antibody molecule disclosed herein does not recognize, e.g., bind to, one or more (e.g., all) of a complementarity determining region (e.g., CDR1, CDR2 and / or CDR3) of a TCRpV protein. In some embodiments, binding of the anti-TCRpV antibody molecule to a TCRPV region results in one, two, three, four, five, six, seven, eight, nine, ten or more (e.g., all) of the following: (i) reduced level, e.g., expression level, and / or activity of IL-1P; (ii) reduced level, e.g., expression level, and / or activity of IL-6; (iii) reduced level, e.g., expression level, and / or activity of TNFa; (iv) increased level, e.g., expression level, and / or activity of IL-2; (v) a delay, e.g., at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 or more hours delay, in increased level, e.g., expression level, and / or activity of IL-2; (vi) a delay, e.g., at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 hours delay, in increased level, e.g., expression level, and / or activity of IFN-gamma; (vii) reduced T cell proliferation kinetics; (viii) reduced cytokine storm, e.g., cytokine release syndrome (CRS) and / or neurotoxicity (NT), e.g., as measured by an assay of Example 3; (ix) cell killing, e.g., target cell killing, e.g. cancer cell killing, e.g., as measured by an assay of Example 4; (x) increased level, e.g., expression level, and / or activity of IL-15; or (xi) increased Natural Killer (NK) cell proliferation, e.g., expansion. In some embodiments, any one or all of (i)-(xi) or any combination thereof resulting from an anti-TCRpV antibody molecule disclosed herein is compared to an antibody that binds to: a CD3 molecule, e.g., CD3 epsilon (CD3e) molecule; or a TCR alpha (TCRa) molecule. In some embodiments, binding of the anti-TCRpV antibody molecule to a TCRpV region results in secretion, e.g., production of perforin and / or Granzyme B. In an aspect, the disclosure provides an antibody molecule which binds, e.g., specifically binds, to a T cell receptor beta variable chain (TCRPV) region, wherein the anti-TCRpV antibody molecule comprises an antigen binding domain comprising: (a) a light chain variable region (VL) comprising: (i) one, two or all of (e.g., three) a light chain complementarity determining region 1 (LC CDR1), a light chain complementarity determining region 2 (LC CDR2), and a light chain complementarity determining region 3 (LC CDR3) of SEQ ID NO: 10 or SEQ ID NO: 11; and (ii) a framework region (FR) having at least 95% identity with one, two, three, or all of (e.g., four) a non-murine germline framework 1 (FR1), a non-murine germline framework region 2 (FR2), a non-murine germline framework region 3 (FR3), and a non-murine germline framework region 4 (FR4); and / or (b) a heavy chain variable region (VH) comprising: (i) one, two or all of (e.g., three) a heavy chain complementarity determining region 1 (HC CDR1), a heavy chain complementarity determining region 2 (HC CDR2) and a heavy chain complementarity determining region 3 (HC CDR3) of SEQ ID NO: 9; and (ii) a framework region (FR) having at least 95% identity with one, two, three, or all of (e.g., four) a non-murine germline framework 1 (FR1), a non-murine germline framework region 2 (FR2), a non-murine germline framework region 3 (FR3), and a non-murine germline framework region 4 (FR4). In some embodiments, the VL comprises a sequence having a consensus sequence of SEQ ID NO: 230 or 3289. In some embodiments, the VH comprises a sequence having a consensus sequence of SEQ ID NO: 231 or 3290. In some embodiments, the anti-TCRpV antibody molecule binds to TCRP V6, e.g., one or more of TCRp V6-4*01, TCRp V6-4*02, TCRp V6-9*01, TCRp V6-8*01, TCRp V6-5*01, TCRp V6-6*02, TCRp V6-6*01, TCRp V6-2*01, TCRp V6-3*01 or TCRp V6-1 *01, or a variant thereof. In some embodiment, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising: (i) a HC CDR1, a HC CDR2 and a HC CDR3 of SEQ ID NO: 1 or SEQ ID NO: 9, or an amino acid sequence listed in Table 1; or (ii) a LC CDR1, a LC CDR2, and a LC CDR3 of SEQ ID NO: 2, SEQ ID NO: 10 or SEQ ID NO: 11, or an amino acid sequence listed in Table 1. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a light chain variable region (VL) comprising one, two or all (e.g., three) of a LC CDR1, a LC CDR2 and a LC CDR3 of SEQ ID NO: 2, SEQ ID NO: 10 or SEQ ID NO: 11, or an amino acid sequence listed in Table 1. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a heavy chain variable region (VH) comprising one, two or all (e.g., three) of a HC CDR1, a HC CDR2 and a HC CDR3 of SEQ ID NO: 1 or SEQ ID NO: 9, or an amino acid sequence listed in Table 1. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising: (i) a VL comprising: a LC CDR1 amino acid sequence of SEQ ID NO: 6 (or an amino acid sequence with not more than 1, 2, 3 or 4 modifications, e.g., substitutions, additions or deletions thereof), a LC CDR2 amino acid sequence of SEQ ID NO:7 (or an amino acid sequence with not more than 1, 2, 3 or 4 modifications, e.g., substitutions, additions or deletions thereof), and / or a LC CDR3 amino acid sequence of SEQ ID NO:8 (or an amino acid sequence with not more than 1, 2, 3 or 4 modifications, e.g., substitutions, additions or deletions thereof); and / or (ii) a VH comprising: a HC CDR1 amino acid sequence of SEQ ID NO: 3 (or an amino acid sequence with not more than 1, 2, 3 or 4 modifications, e.g., substitutions, additions or deletions thereof), a HC CDR2 amino acid sequence of SEQ ID NO:4 (or an amino acid sequence with not more than 1, 2, 3 or 4 modifications, e.g., substitutions, additions or deletions thereof), and / or a HC CDR3 amino acid sequence of SEQ ID NO:5 (or an amino acid sequence with not more than 1, 2, 3 or 4 modifications, e.g., substitutions, additions or deletions thereof). In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising: a variable heavy chain (VH) of an amino acid sequence listed in Table 1, e.g., SEQ ID NO: 9, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to an amino acid sequence listed in Table 1, e.g., SEQ ID NO: 9 or SEQ ID NO: 1312; and / or a variable light chain (VL) of an amino acid sequence listed in Table 1, e.g., SEQ ID NO: 10 or SEQ ID NO: 11, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to an amino acid sequence listed in Table 1, e g., SEQ ID NO: 10 or SEQ ID NO: 11 or SEQ ID NO: 1314. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising: (i) the VH amino acid sequence of SEQ ID NO: 9 or SEQ ID NO: 1312; (ii) an amino acid sequence having at least about 85%, 90%, 95%, or 99% sequence identity to the amino acid sequence of SEQ ID NO: 9 or SEQ ID NO: 1312; (iii) the VL amino acid sequence of SEQ ID NO: 10 or SEQ ID NO: 1314; and / or 7 (iv) an amino acid sequence having at least about 85%, 90%, 95%, or 99% sequence identity to the amino acid sequence of SEQ ID NO: 10 or SEQ ID NO: 1314. In an aspect, provided herein is an antibody molecule which binds, e.g., specifically binds, to a T cell receptor beta variable chain (TCRPV) region, wherein the anti-TCRpV antibody molecule comprises an antigen binding domain comprising: (a) a light chain variable region (VL) comprising: (i) one, two or all of (e.g., three) a light chain complementarity determining region 1 (LC CDR1), a light chain complementarity determining region 2 (LC CDR2), and a light chain complementarity determining region 3 (LC CDR3) of a humanized B-H light chain (LC) of Table 2; and (ii) a framework region (FR) having at least 95% identity with one, two, three or all (e.g., four) of a framework region 1 (FR1), a framework region 2 (FR2), a framework region 3 (FR3), and a framework region 4 (FR4) of a humanized B-H LC of Table 2; and / or (b) a heavy chain variable region (VH) comprising: (i) one, two or all of (e.g., three) a heavy chain complementarity determining region 1 (HC CDR1), a heavy chain complementarity determining region 2 (HC CDR2) and a heavy chain complementarity determining region 3 (HC CDR3) of a humanized B-H heavy chain (HC) of Table 2; and (ii) a framework region (FR) having at least 95% identity with one, two, three or all (e.g., four) of a framework region 1 (FR1), a framework region 2 (FR2), a framework region 3 (FR3), and a framework region 4 (FR4) of a humanized B-H HC of Table 2. In some embodiments, the anti-TCRBV binds to TCRp V12, e.g., TCRp V12-4*01, TCRp V12-3*01, or TCRp V12-5*01, or a variant thereof. In some embodiment, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising: (i) a HC CDR1, a HC CDR2 and a HC CDR3 of Antibody B listed in Table 2; or (ii) a LC CDR1, a LC CDR2, and a LC CDR3 of Antibody B listed in Table 2. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a light chain variable region (VL) comprising one, two or all (e.g., three) of a LC CDR1, a LC CDR2 and a LC CDR3 of a humanized B-H antibody listed in Table 2. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a heavy chain variable region (VH) comprising one, two or all (e.g., three) of a HC CDR1, a HC CDR2 and a HC CDR3 of a humanized B-H antibody listed in Table 2. 8 In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a light chain variable region (VL) comprising one, two or all (e.g., three) of a LC CDR1, a LC CDR2 and a LC CDR3 of a humanized B-H antibody listed in Table 2. In some embodiments, the anti-TCRpV antibody molecule comprises: a VH sequence of a humanized B-H antibody listed in Table 2, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VH of a humanized B-H antibody listed in Table 2; and / or a VL sequence of a humanized B-H antibody listed in Table 2, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VL of a humanized B-H antibody listed in Table 2. In some embodiments, the anti-TCRpV antibody molecule comprises a framework region (FR) having at least 95% identity with one of: a FR1, a FR2, a FR3, and a FR4 of a humanized B-H LC of Table 2. In some embodiments, the anti-TCRpV antibody molecule comprises a framework region (FR) having at least 95% identity with any two of: a FR1, a FR2, a FR3, and a FR4 of a humanized B-HLC of Table 2. In some embodiments, the anti-TCRpV antibody molecule comprises a framework region (FR) having at least 95% identity with any three of: a FR1, a FR2, a FR3, and a FR4 of a humanized B-H LC of Table 2. In some embodiments, the anti-TCRpV antibody molecule comprises a framework region (FR) having at least 95% identity with all of: a FR1, a FR2, a FR3, and a FR4 of a humanized B-H LC of Table 2. In some embodiments, the anti-TCRpV antibody molecule comprises a framework region (FR) having at least 95% identity with one of: a FR1, a FR2, a FR3, and a FR4 of a humanized B-H HC of Table 2. In some embodiments, the anti-TCRpV antibody molecule comprises a framework region (FR) having at least 95% identity with any two of: a FR1, a FR2, a FR3, and a FR4 of a humanized B-H HC of Table 2. In some embodiments, the anti-TCRpV antibody molecule comprises a framework region (FR) having at least 95% identity with any three of: a FR1, a FR2, a FR3, and a FR4 of a humanized B-H HC of Table 2. In some embodiments, the anti-TCRpV antibody molecule comprises a framework region (FR) having at least 95% identity with all of: a FR1, a FR2, a FR3, and a FR4 of a humanized B-H HC of Table 2. In some embodiment, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising: (i) a HC CDR1, a HC CDR2 and a HC CDR3 of Antibody C listed in Table 10; or (ii) a LC CDR1, a LC CDR2, and a LC CDR3 of Antibody C listed in Table 10. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a heavy chain variable region (VH) comprising one, two or all (e.g, three) of a HC CDR1, a HC CDR2 and a HC CDR3 of antibody C or humanized C-H antibody listed in Table 10. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a light chain variable region (VL) comprising one, two or all (e.g., three) of a LC CDR1, a LC CDR2 and a LC CDR3 of antibody C or humanized C-H antibody listed in Table 10. In some embodiments, the anti-TCRpV antibody molecule comprises: a VH sequence of a humanized C-H antibody listed in Table 10, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VH of a humanized C-H antibody listed in Table 10; and / or a VL sequence of a humanized C-H antibody listed in Table 10, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VL of a humanized C-H antibody listed in Table 10. In some embodiment, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising: (i) a HC CDR1, a HC CDR2 and a HC CDR3 of Antibody E listed in Table 11; or (ii) a LC CDR1, a LC CDR2, and a LC CDR3 of Antibody E listed in Table 11. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a heavy chain variable region (VH) comprising one, two or all (e.g., three) of a HC CDR1, a HC CDR2 and a HC CDR3 of antibody E or humanized E-H antibody listed in Table 11. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a light chain variable region (VL) comprising one, two or all (e.g, three) of a LC CDR1, a LC CDR2 and a LC CDR3 of antibody E or humanized E-H antibody listed in Table 11. In some embodiments, the anti-TCRpV antibody molecule comprises: a VH sequence of a humanized E-H antibody listed in Table 11, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VH of a humanized E-H antibody listed in Table 11; and / or a VL sequence of a humanized E-H antibody listed in Table 11, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VL of a humanized E-H antibody listed in Table 11. In some embodiment, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising: (i) a HC CDR1, a HC CDR2 and a HC CDR3 of Antibody D listed in Table 12; or (ii) a LC CDR1, a LC CDR2, and a LC CDR3 of Antibody D listed in Table 12. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a heavy chain variable region (VH) comprising one, two or all (e.g., three) of a HC CDR1, a HC CDR2 and a HC CDR3 of antibody D or humanized D-H antibody listed in Table 12. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a light chain variable region (VL) comprising one, two or all (e.g., three) of a LC CDR1, a LC CDR2 and a LC CDR3 of antibody D or humanized D-H antibody listed in Table 12. In some embodiments, the anti-TCRpV antibody molecule comprises: a VH sequence of a humanized D-H antibody listed in Table 12, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VH of a humanized D-H antibody listed in Table 12; and / or a VL sequence of a humanized D-H antibody listed in Table 12, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VL of a humanized D-H antibody listed in Table 12. In some embodiment, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising: (i) a HC CDR1, a HC CDR2 and a HC CDR3 of Antibody G listed in Table 13; or (ii) a LC CDR1, a LC CDR2, and a LC CDR3 of Antibody G listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a heavy chain variable region (VH) comprising one, two or all (e.g., three) of a HC CDR1, a HC CDR2 and a HC CDR3 of antibody G or humanized G-H antibody listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a light chain variable region (VL) comprising one, two or all (e.g., three) of a LC CDR1, a LC CDR2 and a LC CDR3 of antibody G or humanized G-H antibody listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises: a VH sequence of a humanized G-H antibody listed in Table 13, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VH of a humanized G-H antibody listed in Table 13; and / or a VL sequence of a humanized G-H antibody listed in Table 13, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VL of a humanized G-H antibody listed in Table 13. In some embodiment, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising: (i) a HC CDR1, a HC CDR2 and a HC CDR3 of Antibody H listed in Table 13; or (ii) a LC CDR1, a LC CDR2, and a LC CDR3 of Antibody H listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a heavy chain variable region (VH) comprising one, two or all (e.g., three) of a HC CDR1, a HC CDR2 and a HC CDR3 of antibody H or humanized H-H antibody listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a light chain variable region (VL) comprising one, two or all (e.g.. three) of a LC CDR1, a LC CDR2 and a LC CDR3 of antibody H or humanized H-H antibody listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises: a VH sequence of a humanized H-H antibody listed in Table 13, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VH of a humanized H-H antibody listed in Table 13; and / or a VL sequence of a humanized H-H antibody listed in Table 13, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VL of a humanized H-H antibody listed in Table 13. In some embodiment, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising: (i) a HC CDR1, a HC CDR2 and a HC CDR3 of Antibody I listed in Table 13; or (ii) a LC CDR1, a LC CDR2, and a LC CDR3 of Antibody I listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a heavy chain variable region (VH) comprising one, two or all (e.g., three) of a HC CDR1, a HC CDR2 and a HC CDR3 of antibody I or humanized I-H antibody listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a light chain variable region (VL) comprising one, two or all (e.g., three) of a LC CDR1, a LC CDR2 and a LC CDR3 of antibody I or humanized I-H antibody listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises: a VH sequence of a humanized I-H antibody listed in Table 13, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VH of a humanized I-H antibody listed in Table 13; and / or a VL sequence of a humanized I-H antibody listed in Table 13, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VL of a humanized I-H antibody listed in Table 13. In some embodiment, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising: (i) a HC CDR1, a HC CDR2 and a HC CDR3 of Antibody J listed in Table 13; or (ii) a LC CDR1, a LC CDR2, and a LC CDR3 of Antibody J listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a heavy chain variable region (VH) comprising one, two or all (e.g., three) of a HC CDR1, a HC CDR2 and a HC CDR3 of antibody J or humanized J-H antibody listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a light chain variable region (VL) comprising one, two or all (e.g, three) of a LC CDR1, a LC CDR2 and a LC CDR3 of antibody J or humanized J-H antibody listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises: a VH sequence of a humanized J-H antibody listed in Table 13, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VH of a humanized J-H antibody listed in Table 13; and / or a VL sequence of a humanized J-H antibody listed in Table 13, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VL of a humanized J-H antibody listed in Table 13. In some embodiment, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising: (i) a HC CDR1, a HC CDR2 and a HC CDR3 of Antibody K listed in Table 13; or (ii) a LC CDR1, a LC CDR2, and a LC CDR3 of Antibody K listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a heavy chain variable region (VH) comprising one, two or all (e.g., three) of a HC CDR1, a HC CDR2 and a HC CDR3 of antibody K or humanized K-H antibody listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a light chain variable region (VL) comprising one, two or all (e.g., three) of a LC CDR1, a LC CDR2 and a LC CDR3 of antibody K or humanized K-H antibody listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises: a VH sequence of a humanized G-H antibody listed in Table 13, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VH of a humanized K-H antibody listed in Table 13; and / or a VL sequence of a humanized G-H antibody listed in Table 13, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VL of a humanized K-H antibody listed in Table 13. In some embodiment, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising: (i) a HC CDR1, a HC CDR2 and a HC CDR3 of Antibody L listed in Table 13; or (ii) a LC CDR1, a LC CDR2, and a LC CDR3 of Antibody L listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a heavy chain variable region (VH) comprising one, two or all (e.g., three) of a HC CDR1, a HC CDR2 and a HC CDR3 of antibody L or humanized L-H antibody listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a light chain variable region (VL) comprising one, two or all (e.g., three) of a LC CDR1, a LC CDR2 and a LC CDR3 of antibody L or humanized L-H antibody listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises: a VH sequence of a humanized L-H antibody listed in Table 13, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VH of a humanized L-H antibody listed in Table 13; and / or a VL sequence of a humanized L-H antibody listed in Table 13, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VL of a humanized L-H antibody listed in Table 13. In some embodiment, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising: (i) a HC CDR1, a HC CDR2 and a HC CDR3 of Antibody M listed in Table 13; or (ii) a LC CDR1, a LC CDR2, and a LC CDR3 of Antibody M listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a heavy chain variable region (VH) comprising one, two or all (e.g., three) of a HC CDR1, a HC CDR2 and a HC CDR3 of antibody M or humanized M-H antibody listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a light chain variable region (VL) comprising one, two or all (e.g., three) of a LC CDR1, a LC CDR2 and a LC CDR3 of antibody M or humanized M-H antibody listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises: a VH sequence of a humanized M-H antibody listed in Table 13, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VH of a humanized M-H antibody listed in Table 13; and / or a VL sequence of a humanized M-H antibody listed in Table 13, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VL of a humanized M-H antibody listed in Table 13. In some embodiment, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising: (i) a HC CDR1, a HC CDR2 and a HC CDR3 of Antibody N listed in Table 13; or 15 (ii) a LC CDR1, a LC CDR2, and a LC CDR3 of Antibody N listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a heavy chain variable region (VH) comprising one, two or all (e.g., three) of a HC CDR1, a HC CDR2 and a HC CDR3 of antibody N or humanized N-H antibody listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a light chain variable region (VL) comprising one, two or all (e.g., three) of a LC CDR1, a LC CDR2 and a LC CDR3 of antibody N or humanized N-H antibody listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises: a VH sequence of a humanized N-H antibody listed in Table 13, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VH of a humanized N-H antibody listed in Table 13; and / or a VL sequence of a humanized N-H antibody listed in Table 13, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VL of a humanized N-H antibody listed in Table 13. In some embodiment, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising: (i) a HC CDR1, a HC CDR2 and a HC CDR3 of Antibody O listed in Table 13; or (ii) a LC CDR1, a LC CDR2, and a LC CDR3 of Antibody O listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a heavy chain variable region (VH) comprising one, two or all (e.g., three) of a HC CDR1, a HC CDR2 and a HC CDR3 of antibody O or humanized O-H antibody listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a light chain variable region (VL) comprising one, two or all (e.g., three) of a LC CDR1, a LC CDR2 and a LC CDR3 of antibody O or humanized O-H antibody listed in Table 13. In some embodiments, the anti-TCRpV antibody molecule comprises: a VH sequence of a humanized O-H antibody listed in Table 13, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VH of a humanized O-H antibody listed in Table 13; and / or a VL sequence of a humanized O-H antibody listed in Table 13, or a sequence having at least about 85%, 90%, 95%, or 99% sequence identity to a VL of a humanized O-H antibody listed in Table 13. In another aspect, the disclosure provides a non-murine, e.g., a human-like antibody molecule (e.g., a human or humanized antibody molecule), which binds, e.g., specifically binds, to a T cell receptor beta variable (TCRPV) region. In some embodiments, binding of the anti-TCRPV antibody molecule results in expansion, e.g., at least about 1.1-50 fold expansion (e.g., at least about 1.5-40 fold, 2-35 fold, 3-30 fold, 5-25 fold, 8-20 fold, or 10-15 fold expansion), of a population of T cells, e.g., a population of T cells having a memory-like phenotype, e.g., CD45RA+ CCR7- T cells. In some embodiments, the population of T cells having a memorylike phenotype comprises CD4+ and / or CD8+ T cells. In some embodiments, the population of T cells having a memory-like phenotype comprises a population of memory T cells, e.g., T effector memory (Tem) cells, e.g., Tem cells expressing CD45RA (Temra) cells, e.g., CD4+ or CD8+ Temra cells. In some embodiments, the population of T cells having a memory-like phenotype does not express a senescent marker, e.g., CD57. In some embodiments, the population of T cells having a memory-like phenotype does not express an inhibitory receptor, e.g., OX40, 4-1BB, and / or ICOS. In some embodiments, the population of T cells having a memory-like phenotype is a population of T cells with CD45RA+ CCR7- CD57-. In some embodiments, the population of T cells having a memory-like phenotype does not express an inhibitory receptor, e.g., OX40, 4-1BB, and / or ICOS. In some embodiments, the population of T cells having a memory-like phenotype, e.g., as described herein, has increased proliferative capacity, e.g., as compared to a reference cell population, e.g., an otherwise similar population of cells that has not been contacted with an anti-TCRpV antibody. In some embodiments, the expansion is at least about 1.1-10 fold expansion (e.g., at least about 1.1, 1.2, 1.3, 1.4, 1.5, 2, 3, 4, 5, 6, 7, 8, 9, or 10 fold expansion). In some embodiments, expansion of the population of T cells having a memory-like phenotype, e.g., memory effector T cells, e.g., Tem cells, e.g., Temra cells, e.g., CD4+ or CD8+ Temra cells, is compared to expansion of a similar population of cells with an antibody that binds to: a CD3 molecule, e.g., CD3 epsilon (CD3e) molecule; or a TCR alpha (TCRa) molecule. In some embodiments, the population of expanded T cells having a memory-like phenotype, e.g., T effector memory cells, comprises cells T cells, e.g., CD3+, CD8+ or CD4+ T 17 cells. In some embodiments, the population of expanded T cells having a memory-like phenotype, T effector memory cells, comprises CD3+ and CD8+ T cells. In some embodiments, the population of expanded T cells having a memory-like phenotype, e.g., T effector memory cells comprises CD3+ and CD4+ T cells. In some embodiments, the population of expanded T cells having a memory-like phenotype, T effector memory (Tem) cells, comprises cells T cells, e.g., CD3+, CD8+ or CD4+ T cells, which express or re-express, CD45RA, e.g., CD45RA+. In some embodiments, the population comprises Tem cells expressing CD45RA, e.g., Temra cells. In some embodiments, expression of CD45RA on Temra cells, e.g., CD4+ or CD8+ Temra cells, can be detected by a method disclosed herein, e.g., flow cytometry. In some embodiments, the population of T cells having a memory-like phenotype, e.g., Temra cells have low or no expression of CCR7, e.g., CCR7- or CCR7 low. In some embodiments, expression of CCR7 on Temra cells cannot be detected by a method disclosed herein, e.g., flow cytometry. In some embodiments, the population of T cells having a memory-like phenotype, e.g., Temra cells express CD95, e.g., CD95+. In some embodiments, expression of CD95 on Temra cells can be detected by a method disclosed herein, e.g., flow cytometry. In some embodiments, the population of T cells having a memory-like phenotype, e.g., Temra cells express CD45RA, e.g., CD45RA+, have low or no expression of CCR7, e.g., CCR7-or CCR7 low, and express CD95, e.g., CD95+. In some embodiments, the population of T cells having a memory-like phenotype, e.g., Temra cells can be identified as CD45RA+, CCR7- and CD95+ cells. In some embodiments, the population of T cells having a memory-like phenotype, e.g., Temra cells comprise CD3+, CD4+ or CD8+ T cells (e.g., CD3+ T cells, CD3+ CD8+ T cells, or CD3+ CD4+ T cells). In some embodiments, the population of T cells having a memory-like phenotype does not express a senescent marker, e.g., CD57. In some embodiments, the population of T cells having a memory-like phenotype does not express an inhibitory receptor, e.g., 0X40, 4-1BB, and / or ICOS. In some embodiments, binding of the anti-TCRpV antibody molecule results in expansion, e.g., at least about 1.1-50 fold expansion (e.g., at least about 1.5-40 fold, 2-35 fold, 3-30 fold, 5-25 fold, 8-20 fold, or 10-15 fold expansion), of a subpopulation of T cells. In some embodiments, the anti-TCRpV antibody molecule-activated (e.g., expanded) subpopulation of T cells resemble Temra cells in high expression of CD45RA and / or low expression of CCR7. In some embodiments, the anti-TCRpV antibody molecule-activated (e.g., expanded) 18 subpopulation of T cells do not display upregulation of the senescence markers CD57 and / or KLRG1. In some embodiments, the anti-TCRpV antibody molecule-activated (e.g., expanded) subpopulation of T cells do not display upregulation of co-stimulatory molecules CD27 and / or CD28. In some embodiments, the anti-TCRpV antibody molecule-activated (e.g., expanded) subpopulation of T cells are highly proliferative. In some embodiments, the anti-TCRpV antibody molecule-activated (e.g., expanded) subpopulation of T cells secrete IL-2. In some embodiments, expression of surface markers on T cells can be detected by a method disclosed herein, e.g., flow cytometry. In some embodiments, the proliferative capability of T cells can be detected by a method disclosed herein, e.g., a method described in Example 4. In some embodiments, cytokine expression of T cells can be detected by a method disclosed herein, e.g., a method described in Examples 10 and 21. In some embodiments, the expansion is at least about 1.1-10 fold expansion (e.g., at least about 1.1, 1.2, 1.3, 1.4, 1.5, 2, 3, 4, 5, 6, 7, 8, 9, or 10 fold expansion). In some embodiments, the expansion is compared to expansion of a similar population of cells with an antibody that binds to a CD3 molecule, e.g., CD3 epsilon (CD3e) molecule; or a TCR alpha (TCRa) molecule. In some embodiments, binding of the anti-TCRpV antibody molecule to a TCRPV region results in one, two, three, four, five, six, seven, eight, nine, ten or more (e.g., all) of the following: (i) reduced level, e.g., expression level, and / or activity of IL-1P; (ii) reduced level, e.g., expression level, and / or activity of IL-6; (iii) reduced level, e.g., expression level, and / or activity of TNFa; (iv) increased level, e.g., expression level, and / or activity of IL-2; (v) a delay, e.g., at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 or more hours delay, in increased level, e.g., expression level, and / or activity of IL-2; (vi) a delay, e.g., at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 hours delay, in increased level, e.g., expression level, and / or activity of IFNg; (vii) reduced T cell proliferation kinetics; (viii) reduced cytokine storm, e.g., cytokine release syndrome (CRS) and / or neurotoxicity (NT), e.g., as measured by an assay of Example 3; (ix) cell killing, e.g., target cell killing, e.g. cancer cell killing, e.g., as measured by an assay of Example 4; (x) increased level, e.g., expression level, and / or activity of IL-15; or (xi) increased Natural Killer (NK) cell proliferation, e.g., expansion, compared to an antibody that binds to: a CD3 molecule, e.g., CD3 epsilon (CD3e) molecule; or a TCR alpha (TCRa) molecule. In some embodiments of any of the compositions disclosed herein, binding of the anti-TCRPV antibody molecule to a TCRPV region results in a reduction of at least 2, 5, 10, 20, 50, 100, or 200 fold, or at least 2-200 fold (e.g., 5-150, 10-100, 20-50 fold) in the expression level and or activity of IL-ip as measured by an assay of Example 3. In some embodiments of any of the compositions disclosed herein, binding of the anti-TCRPV antibody molecule to a TCRPV region results in a reduction of at least 2, 5, 10, 20, 50, 100, 200, 300, 400, 500, 600, 700, 800, 900, or 1000 fold, or at least 2-1000 fold (e.g., 5-900, 10-800, 20-700, 50-600, 100-500, or 200-400 fold) in the expression level and or activity of IL-6 as measured by an assay of Example 3. In some embodiments of any of the compositions disclosed herein, binding of the anti-TCRPV antibody molecule to a TCRPV region results in a reduction of at least 2, 5, 10, 20, 50, 100, 200, 300, 400, 500, 600, 700, 800, 900, 1000, or 2000 fold, or at least 2-2000 fold (e.g, 5-1000, 10-900, 20-800, 50-700, 100-600, 200-500, or 300-400 fold) in the expression level and or activity of TNFa as measured by an assay of Example 3. In some embodiments of any of the compositions disclosed herein, binding of the anti-TCRPV antibody molecule to a TCRPV region results in an increase of at least 2, 5, 10, 20, 50, 100, 200, 300, 400, 500, 600, 700, 800, 900, 1000, or 2000 fold, or at least 2-2000 fold (e.g., 5-1000, 10-900, 20-800, 50-700, 100-600, 200-500, or 300-400 fold) in the expression level and or activity of IL-2 as measured by an assay of Example 3. In some embodiments of any of the compositions disclosed herein, binding of the anti-TCRPV antibody molecule to a TCRPV region results in an increase of at least 2, 5, 10, 20, 50, 100, 200, 300, 400, 500, 600, 700, 800, 900, 1000, or 2000 fold, or at least 2-2000 fold (e.g., 5-1000, 10-900, 20-800, 50-700, 100-600, 200-500, or 300-400 fold) in the expression level and or activity of IL-15 as measured by an assay of Example 4. In some embodiments of any of the compositions disclosed herein, binding of the anti-TCRPV antibody molecule results in proliferation, e.g., expansion, e.g., at least about 1.1-50 fold expansion (e.g., at least about 1.5-40 fold, 2-35 fold, 3-30 fold, 5-25 fold, 8-20 fold, or 10-15 fold expansion), of a population of Natural Killer (NK) cells. In some embodiments, the expansion of NK cells is at least about 1.1-30 fold expansion (e.g., at least about 1.1, 1.2, 1.3, 1.4, 1.5,2,3,4, 5,6, 7, 8, 9, 10, 15,20, 25, or at least about 1.1-5, 5-10, 10-15, 15-20, 20-25, or 25-30 fold expansion). In some embodiments, the expansion of NK cells is measure by an assay of Example 4. In some embodiments, the expansion of NK cells by, e.g., binding of, the anti-20 TCRPV antibody molecule is compared to expansion of an otherwise similar population not contacted with the anti-TCRpv antibody molecule. In some embodiments of any of the compositions disclosed herein, binding of the anti-TCRPV antibody molecule results in cell killing, e.g., target cell killing, e.g. cancer cell killing. In some embodiments, the cancer cell is a hematological cancer cell or a solid tumor cell. In some embodiments, the cancer cell is a multiple myeloma cell. In some embodiments, binding of the anti-TCRpV antibody molecule results in cell killing in vitro or in vivo. In some embodiments, cell killing is measured by an assay of Example 4. In some embodiments of any of the compositions disclosed herein, binding of the anti-TCRpV antibody molecule to a TCRpV region results in an increase or decrease of at least 2, 5, 10, 20, 50, 100, 200, 300, 400, 500, 600, 700, 800, 900, 1000, or 2000 fold, or at least 2-2000 fold (e.g., 5-1000, 10-900, 20-800, 50-700, 100-600, 200-500, or 300-400 fold) of any of the activities described herein compared the activity of 16G8 or TM23 murine antibody, or a humanized version thereof as described in US Patent 5,861,155. In an aspect, provided herein is an antibody molecule which binds, e.g., specifically binds, to a T cell receptor beta variable chain (TCRPV) region (an anti-TCRpV antibody molecule), wherein the anti-TCRpV antibody molecule: (i) binds specifically to an epitope on TCRPV, e.g., the same or similar epitope as the epitope recognized by an anti-TCRpV antibody molecule as described herein, e.g., a second anti-TCRpV antibody molecule; (ii) shows the same or similar binding affinity or specificity, or both, as an anti-TCRpV antibody molecule as described herein, e.g., a second anti-TCRpV antibody molecule; (iii) inhibits, e.g., competitively inhibits, the binding of an anti-TCRpV antibody molecule as described herein, e.g., a second anti-TCRpV antibody molecule; (iv) binds the same or an overlapping epitope with an anti-TCRpV antibody molecule as described herein, e.g., a second anti-TCRpv antibody molecule; or (v) competes for binding, and / or binds the same epitope, with an anti-TCRpV antibody molecule as described herein, e.g., a second anti-TCRpv antibody molecule, In some embodiments, the second anti-TCRpv antibody molecule comprises an antigen binding domain chosen from Table 1 or Table 2, or a sequence substantially identical thereto. In some embodiments, the second anti-TCRpv antibody molecule comprises an antigen binding domain, comprising: a heavy chain complementarity determining region 1 (HC CDR1), a heavy chain complementarity determining region 2 (HC CDR2) and / or a heavy chain complementarity 21 determining region 3 (HC CDR3) of SEQ ID NO: 1 or SEQ ID NO: 9; and / or a light chain complementarity determining region 1 (LC CDR1), a light chain complementarity determining region 2 (LC CDR2), and / or a light chain complementarity determining region 3 (LC CDR3) of SEQ ID NO: 2, SEQ ID NO: 10 or SEQ ID NO: 11. In some embodiments of any of the compositions disclosed herein, binding of the anti-TCRPV antibody molecule to a TCRPV region results in a change in any (e.g., one, two, three, four or all) of (i)-(v) that is different, e.g., an increase or decrease, of at least 2, 5, 10, 20, 50, 100-fold, compared the activity of 16G8 or TM23 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments of any of the compositions disclosed herein, the anti-TCRpV antibody molecule binds to a TCRBV family (e.g., gene family), e.g., a TCRBV gene family comprising subfamilies, e.g., as described herein. In some embodiments, the TCRBV family, e.g., gene family, comprises: a TCRP V6 subfamily, a TCRP V10 subfamily, a TCRP V12 subfamily, a TCRP V5 subfamily, a TCRp V7 subfamily, a TCRp Vil subfamily, a TCRp VI4 subfamily, a TCRp V16 subfamily, a TCRp VI8 subfamily, a TCRp V9 subfamily, a TCRp V13 subfamily, a TCRp V4 subfamily, a TCRP V3 subfamily, a TCRp V2 subfamily, a TCRP VI5 v, a TCRp V30 subfamily, a TCRp V19 subfamily, a TCRp V27 subfamily, a TCRp V28 subfamily, a TCRP V24 subfamily, a TCRP V20 subfamily, TCRp V25 subfamily, a TCRp V29 subfamily, a TCRp V23 subfamily, a TCRp V21 subfamily, a TCRp VI subfamily, a TCRp VI7 subfamily, or a TCRP V26 subfamily. In some embodiments, the anti-TCRpV antibody binds to a TCRP V6 subfamily chosen from: TCRp V6-4*01, TCRp V6-4*02, TCRp V6-9*01, TCRp V6-8*01, TCRp V6-5*01, TCRp V6-6*02, TCRp V6-6*01, TCRp V6-2*01, TCRp V6-3*01 or TCRp V6-l*01. In some embodiments the TCRp V6 subfamily comprises TCRp V6-5*01. In some embodiments, the anti-TCRpV antibody binds to a TCRP VI0 subfamily chosen from: TCRp V10-l*01, TCRp V10-l*02, TCRp V10-3*01 or TCRp V10-2*01. In some embodiments, the anti-TCRpV antibody binds to a TCRP V12 subfamily chosen from: TCRp V12-4*01, TCRp V12-3*01 or TCRp V12-5*01. In some embodiments of any of the compositions disclosed herein, the anti-TCRpV antibody molecule does not bind to TCRp V12, or binds to TCRp V12 with an affinity and / or binding specificity that is less than (e.g., less than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the 16G8 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments of any of the compositions disclosed herein, the anti-TCRpV antibody molecule binds to TCRP V12 with an affinity and / or binding specificity that is greater than (e.g., greater than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the 16G8 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments of any of the compositions disclosed herein, the anti-TCRpV antibody molecule binds to a TCRPV region other than TCRP ¥12 (e.g., TCRPV region as described herein, e.g., TCRP V6 subfamily (e.g., TCRP V6-5*01) with an affinity and / or binding specificity that is greater than (e.g., greater than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the 16G8 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments of any of the compositions disclosed herein, the anti-TCRpV antibody molecule does not comprise at least one CDR of Antibody B. In some embodiments of any of the compositions disclosed herein, the anti-TCRpV antibody molecule does not comprise the CDRs of Antibody B. In some embodiments of any of the compositions disclosed herein, the anti-TCRpV antibody binds to a TCRP V5 subfamily chosen from: TCRP ¥5-5*01, TCRP ¥5-6*01, TCRP ¥5-4*01, TCRP ¥5-8*01, TCRp ¥5-1*01. In some embodiments of any of the compositions disclosed herein, the anti-TCRP¥ antibody binds to a TCRP ¥5 subfamily chosen from: TCRp ¥5-5*01, TCRP ¥5-6*01, TCRP ¥5-4*01, TCRp ¥5-8*01, TCRp ¥5-1*01. In some embodiments of any of the compositions disclosed herein, the anti-TCRp¥ antibody molecule does not bind to TCRP ¥5-5*01 or TCRP ¥5-1*01, or binds to TCRP ¥5-5*01 or TCRp ¥5-1*01 with an affinity and / or binding specificity that is less than (e.g., less than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the TM23 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments of any of the compositions disclosed herein, the anti-TCRp¥ antibody molecule binds to TCRP ¥5-5*01 or TCRP ¥5-l*01with an affinity and / or binding specificity that is greater than (e.g., greater than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the TM23 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments of any of the compositions disclosed herein, the anti-TCRP¥ antibody molecule binds to a TCRPV region other than TCRP ¥5-5*01 or TCRP ¥5-1*01 (e.g., TCRPV region as described herein, e.g., TCRP ¥6 subfamily (e.g., TCRP V6-5*01) with an affinity and / or binding specificity that is greater than (e.g., greater than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the TM23 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments of any of the compositions disclosed herein, the anti-TCRpV antibody molecule does not comprise at least one CDR of the TM23 murine antibody. In some embodiments of any of the compositions disclosed herein, the anti-TCRpV antibody molecule does not comprise the CDRs of the TM23 murine antibody. In some embodiments of any of the compositions disclosed herein, an anti-TCRpV antibody molecule disclosed herein does not comprise the sequence of a murine anti-rat TCR antibody R73, e.g., as disclosed in J Exp Med. 1989 Jan 1; 169(1): 73-86, herein incorporated by reference in its entirety. In some embodiments of any of the compositions disclosed herein, a multispecific antibody molecule disclosed herein does not comprise the sequence of a murine anti-rat TCR antibody R73, e.g., as disclosed in J Immunol. 1993 Mar 15; 150(6):2305-15, herein incorporated by reference in its entirety. In some embodiments of any of the compositions disclosed herein, an anti-TCRpV antibody molecule disclosed herein does not comprise a viral peptide-MHC complex, e.g., as disclosed in Oncoimmunology. 2016; 5(1): el052930, herein incorporated by reference in its entirety. In some embodiments of any of the compositions disclosed herein, a multispecific antibody molecule disclosed herein does not comprise a viral peptide-MHC complex, e.g., as disclosed in Oncoimmunology. 2016; 5(1): el052930, herein incorporated by reference in its entirety. In some embodiments of any of the compositions disclosed herein, the anti-TCRp¥ antibody molecule binds to one or more (e.g., all) of the following TCRp¥ subfamilies: (i) TCRp ¥6 subfamily comprising, e.g., one or more of TCRP ¥6-4*01, TCRP ¥6-4*02, TCRp ¥6-9*01, TCRp ¥6-8*01, TCRp ¥6-5*01, TCRp ¥6-6*02, TCRp ¥6-6*01, TCRp ¥6-2*01, TCRP ¥6-3*01 or TCRp ¥6-1*01; (ii) TCRP ¥10 subfamily comprising, e.g., one or more of TCRP ¥10-1*01, TCRp ¥10-1*02, TCRp ¥10-3*01 or TCRp ¥10-2*01; (iii) TCRP ¥5 subfamily comprising, e.g., one or more of TCRP ¥5-6*01, TCRP ¥5-4*01, or TCRp ¥5-8*01; (iv) TCRP ¥12 subfamily comprising e.g., one or more of TCRp ¥12-4*01, TCRp ¥12-3*01, or TCRp V12-5*01; (v) TCRP ¥7 subfamily comprising e.g., one or more of TCRP V7-7*01, TCRp ¥7-6*01, TCRp ¥7 -8*02, TCRp ¥7 -4*01, TCRp V7-2*02, TCRp ¥7-2*03, TCRp ¥7-2*01, TCRp ¥7-3*01, TCRp ¥7-9*03, or TCRp ¥7-9*01; (vi) TCRP ¥11 subfamily comprising e.g., one or more of TCRp ¥11-1*01, TCRp ¥11-2*01 or TCRp ¥11-3*01; (vii) TCRP ¥14 subfamily comprising TCRp ¥14*01; (viii) TCRP ¥16 subfamily comprising TCRP ¥16*01; (ix) TCRp ¥18 subfamily comprising TCRp ¥18*01; (x) TCRp ¥9 subfamily comprising T e.g., one or more of CRP ¥9*01 or TCRp ¥9*02; (xi) TCRp ¥13 subfamily comprising TCRp ¥13*01; (xii) TCRP ¥4 subfamily comprising e.g., one or more of e.g., one or more of TCRP ¥4-2*01, TCRp ¥4-3*01, or TCRp ¥4-1*01; (xiii) TCRP ¥3 subfamily comprising TCRP ¥3-1*01; (xiv) TCRP ¥2 subfamily comprising TCRp ¥2*01; (xv) TCRp ¥15 subfamily comprising TCRP ¥15*01; (xvi) TCRp ¥30 subfamily comprising e.g., one or more of TCRP ¥30*01, or TCRP ¥30*02; (xvii) TCRP ¥19 subfamily comprising e.g., one or more of TCRP ¥19*01, or TCRP ¥19*02; (xviii) TCRp ¥27 subfamily comprising TCRp ¥27*01; (xix) TCRp ¥28 subfamily comprising TCRp ¥28*01; (xx) TCRP ¥24 subfamily comprising TCRP ¥24-1*01; (xxi) TCRP ¥20 subfamily comprising e.g., one or more of TCRP ¥20-1*01, or TCRP ¥20-1*02; (xxii) TCRP ¥25 subfamily comprising TCRp ¥25-1*01; or (xxiii) TCRp ¥29 subfamily comprising TCRp ¥29-1*01; (xxiv) TCRP ¥21 subfamily; (xxv) TCRp ¥1 subfamily; (xxvi) TCRp ¥17 subfamily; (xvii) TCRP ¥23 subfamily; or (xviii) TCRp ¥26 subfamily. In some embodiments of any of the compositions disclosed herein, the anti-TCRP¥ antibody molecule binds to one or more (e.g., all) of the following TCRPV subfamilies: (i) TCRp V6, e.g., one or more of TCRp ¥6-4*01, TCRp ¥6-4*02, TCRp ¥6-9*01, TCRp ¥6-8*01, TCRp ¥6-5*01, TCRp ¥6-6*02, TCRp ¥6-6*01, TCRp ¥6-2*01, TCRp ¥6-3*01 or TCRp ¥6-1*01; (ii) TCRp V10, e.g., one or more of TCRp ¥10-1*01. TCRp ¥10-1*02, TCRp ¥10-3*01 or TCRp ¥10-2*01; (iii) TCRp ¥12, e.g., one or more of TCRp ¥12-4*01, TCRp ¥12-3*01, or TCRp ¥12-5*01; or (iv) TCRp ¥5, e.g., one or more of TCRp ¥5-5*01, TCRp ¥5-6*01, TCRp ¥5-4*01, TCRp ¥5-8*01, TCRp ¥5-1*01. In some embodiments, the anti-TCRp¥ antibody molecule binds to TCRP ¥6, e.g., one or more of TCRP ¥6-4*01, TCRp ¥6-4*02, TCRp ¥6-9*01, TCRp ¥6-8*01, TCRp ¥6-5*01, TCRp ¥6-6*02, TCRp ¥6-6*01, TCRp ¥6-2*01, TCRp ¥6-3*01 or TCRp ¥6-1*01. In some embodiments, the anti-TCRp¥ antibody molecule binds to TCRp ¥6-5*01. In some embodiments, the anti-TCRp¥ antibody molecule does not bind to TCRp ¥12. In some embodiments, the anti-TCRP¥ antibody molecule does not bind to TCRP ¥5-5*01 or TCRp ¥5-1*01. In an aspect, provided herein is a multispecific molecule (e.g., a bispecific molecule), comprising a first moiety (e.g., a first immune cell engager) comprising an antibody molecule which binds (e.g., specifically binds) to a T cell receptor beta variable region (TCRp¥) (“anti-TCRp¥ antibody molecule”). In some embodiments, the multispecific molecule comprises a second moiety which comprises one or more of: a tumor-targeting moiety, a cytokine molecule, a stromal modifying moiety, or an anti-TCRp¥ antibody molecule other than the first moiety. In some embodiments, binding of the first moiety to the TCRp¥ region results in a cytokine profile, e.g., cytokine secretion profile, that differs from that of a T cell engager that binds to a receptor or molecule other than a TCRP¥ region (“a non-TCRp¥-binding T cell engager”). In another aspect, the disclosure provides a multispecific molecule, e.g., a bispecific molecule, comprising the anti-TCRp¥ antibody molecule disclosed herein. In some embodiments, the multispecific molecule further comprises: a tumor-targeting moiety, a cytokine molecule, an immune cell engager, e.g., a second immune cell engager, and / or a stromal modifying moiety. In yet another aspect, disclosed herein is a multispecific molecule, e.g., a bispecific molecule, comprising: (i) a first moiety comprising a first immune cell engager comprising an anti-TCRpV antibody molecule disclosed herein; and (ii) a second moiety comprising one or more of: a tumor-targeting moiety; a second immune cell engager; a cytokine molecule or a stromal modifying moiety. In another aspect, the disclosure provides an isolated nucleic acid molecule comprising a nucleotide sequence encoding an anti-TCRpV antibody molecule disclosed herein, or a nucleotide sequence having at least 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. In another aspect, the disclosure provides an isolated nucleic acid molecule comprising a nucleotide sequence encoding a multispecific molecule disclosed herein, or a nucleotide sequence having at least 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. In yet another aspect, the disclosure provides a vector, e.g., an expression vector, comprising a nucleotide sequence encoding an anti-TCRpV antibody molecule disclosed herein, or a nucleotide sequence having at least 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. In another aspect, the disclosure provides a vector, e.g., an expression vector, comprising a nucleotide sequence encoding a multispecific molecule disclosed herein, or a nucleotide sequence having at least 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. In one aspect, the disclosure provides a cell, e.g., host cell, e.g., a population of cells, comprising a nucleic acid molecule encoding an anti-TCRpV antibody molecule disclosed herein, or a nucleotide sequence having at least 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. In some embodiments, the cell or population of cells comprising a nucleic acid molecule encoding anti-TCRpV antibody molecule, comprises: (i) a heavy chain comprising: a variable region (VH), e.g., a VH listed in Tables 1-2 or 10-13, or a sequence having at least 75%, 80%, 85%, 90%, 95%, or 99% identity thereto; and one or more heavy chain constant regions, e.g., as described herein; and / or (ii) a light chain comprising: a variable region (VL) e.g., a VL listed in 27 Tables 1-2 or 10-13, or a sequence having at least 75%, 80%, 85%, 90%, 95%, or 99% identity thereto; and a light chain constant region, e.g, as described herein, e.g., a kappa chain constant region comprising the sequence of SEQ ID NO: 39, or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto. In some embodiments, the cell or population of cells further comprises an IgJ heavy chain constant region or a fragment thereof. In some embodiments, the IgJ heavy chain constant region comprises the sequence of SEQ ID NO: 76 or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto. In some embodiments, the IgJ is comprised in, e.g., expressed in, the same cell or population of cells comprising, e.g., expressing, the anti-TCRpV antibody molecule, e.g., the heavy chain and / or the light chain of the anti-TCRpV antibody molecule. In some embodiments, the IgJ is expressed in a different cell or population of cells than the cell or population of cells comprising, e.g., expressing, the anti-TCRpV antibody molecule, e.g., the heavy chain and / or the light chain of the anti-TCRpV antibody molecule. In one aspect, the disclosure provides a cell, e.g., host cell, e.g., a population of cells, comprising a nucleic acid molecule encoding a multispecific molecule disclosed herein, or a nucleotide sequence having at least 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. In one aspect, disclosed herein is an anti-TCRpV antibody molecule for use in the manufacture of a medicament for treating a disease, e.g., cancer, in a subject. In one aspect, disclosed herein is a multispecific molecule comprising an anti-TCRpV antibody molecule for use in the manufacture of a medicament for treating a disease, e.g., cancer, in a subject. In another aspect, the disclosure provides a method of making, e.g., producing, an anti-TCRpV antibody molecule, a multispecific molecule described herein, comprising culturing a host cell described herein, under suitable conditions. In some embodiments of a method of making a multispecific molecule, the conditions comprise, e.g., conditions suitable for gene expression and / or homo- or heterodimerization. In another aspect, the disclosure provides a pharmaceutical composition comprising an anti-TCRpV antibody molecule, or a multispecific molecule described herein, and a pharmaceutically acceptable carrier, excipient, or stabilizer. In an aspect, the disclosure provides a method of modulating, e.g., enhancing, an immune response in a subject comprising administering to the subject an effective amount of an antibody molecule which binds (e.g., specifically binds) to a T cell receptor beta variable region (TCRPV) (“anti-TCRpV antibody molecule”). In an aspect, the disclosure provides a method of modulating, e.g., enhancing, an immune response in a subject comprising administering to the subject an effective amount of a multispecific molecule disclosed herein. In some embodiments, the method comprises expanding, e.g., increasing the number of, an immune cell population in the subject. In an aspect, the disclosure provides a method of expanding, e.g., increasing the number of, an immune cell population comprising, contacting the immune cell population with an effective amount of an antibody molecule which binds (e.g., specifically binds) to a T cell receptor beta variable region (TCRPV) (“anti-TCRpV antibody molecule”). In an aspect, the disclosure provides a method of expanding, e.g., increasing the number of, an immune cell population comprising, contacting the immune cell population with an effective amount of a multispecific molecule disclosed herein. In some embodiments, the expansion occurs in vivo or ex vivo (e.g., in vitro). In some embodiments, the immune cell population comprises a TCRPV expressing cell, e.g., a TCRPV+ cell. In some embodiments, the TCRpV expressing cell is a T cell, e.g., a CD8+ T cell, a CD3+ T cell or a CD4+ T cell. In some embodiments, the immune cell population comprises a T cell (e.g., a CD4 T cell, or a CD8 T cell). In some embodiments, the immune cell population comprises a T cell having a memory-like phenotype, e.g., CD45RA+ CCR7-. In some embodiments, the immune cell population comprises an effector T cell or a memory T cell (e.g., a memory effector T cell (e.g., TEM cell, e.g., TEMRA cell), or a tumor infiltrating lymphocyte (TIL)). In some embodiments, the immune cell population comprises a T cell, a Natural Killer cell, a B cell, or a myeloid cell. In some embodiments, the immune cell population is obtained from a healthy subject. In an aspect, provided herein is a method of treating a disease e.g., cancer, in a subject comprising administering to the subject an effective amount, e.g., a therapeutically effective amount, of an anti-TCRpV antibody molecule or a multispecific molecule comprising an anti-TCRPV antibody molecule disclosed herein, thereby treating the disease. In a related aspect, provided herein is a composition comprising an anti-TCRpV antibody molecule or a multispecific molecule comprising an anti-TCRpV antibody molecule disclosed herein, for use in the treatment of a disease, e.g., cancer, in a subject. In some embodiments, the disease is a cancer, e.g., a solid tumor or a hematological cancer, or a metastatic lesion. In some embodiments, the method further comprises administering a second agent, e.g., therapeutic agent, e.g., as described herein. In some embodiments, second agent comprises a therapeutic agent (e.g., a chemotherapeutic agent, a biologic agent, hormonal therapy), radiation, or surgery. In some embodiments, therapeutic agent is selected from: a chemotherapeutic agent, or a biologic agent. In another aspect, provided herein is a method of targeting, e.g., directing or re-directing, a therapy, e.g., treatment, to a T cell, e.g., in a subject, e.g., having a disease, e.g., cancer, comprising administering an effective amount of: (i) an anti-TCRpV antibody disclosed herein; and (ii) the therapy, e.g., a tumor targeting therapy (e.g., an antibody that binds to a cancer antigen), e.g., as described herein, thereby targeting the T cell. In some embodiments, (i) and (ii) are conjugated, e.g., linked. In some embodiments, (i) and (ii) are administered simultaneously or concurrently. In some embodiments, the method results in: reduced cytokine release syndrome (CRS) (e.g., lesser duration of CRS or no CRS), or a reduced severity of CRS (e.g., absence of severe CRS, e.g., CRS grade 4 or 5) compared to administration of (ii) alone. In some embodiments, CRS is assessed by an assay of Example 3. In some embodiments, the method results in: reduced neurotoxicity (NT) (e.g., lesser duration of NT or no NT), or a reduced severity of NT (e.g., absence of severe NT) compared to administration of (ii) alone. In yet another aspect, the disclosure provides, a method of targeting a T cell, e.g., in a subject having a disease, e.g., cancer, with an anti-TCRpV antibody disclosed herein or a multispecific molecule comprising an anti-TCRpV antibody disclosed herein. In another aspect, the disclosure provides a method of treating, e.g., preventing or reducing, cytokine release syndrome (CRS) and / or neurotoxicity (NT) in a subject, e.g., CRS and / or NT associated with a treatment, e.g., a previously administered treatment, comprising 30 administering to the subject an effective amount of an anti-TCRpV antibody disclosed herein or a multispecific molecule comprising an anti-TCRpV antibody disclosed herein, wherein, the subject has a disease, e.g, a cancer, thereby treating, e.g., preventing or reducing, CRS and / or NT in the subject. In a related aspect, the disclosure provides a composition comprising an anti-TCRpV antibody disclosed herein or a multispecific molecule comprising an anti-TCRpV antibody disclosed herein, for use in the treatment, e.g., prevention or reduction, of cytokine release syndrome (CRS) and / or neurotoxicity (NT) in a subject, e.g., CRS and / or NT associated with a treatment, e.g., a previously administered treatment, comprising administering to the subject an effective amount of the anti-TCRpV antibody, wherein the subject has a disease, e.g., a cancer. In some embodiments of a method or composition for use disclosed herein, the anti-TCRPV antibody is administered concurrently with or after the administration of the treatment associated with CRS and / or NT. In another aspect, provided herein is a method of expanding, e.g., increasing the number of, an immune cell population comprising, contacting the immune cell population with an antibody molecule, e.g., humanized antibody molecule, which binds, e.g., specifically binds, to a T cell receptor beta variable chain (TCRPV) region (e.g., anti-TCRpV antibody molecule described herein or a multispecific molecule comprising an anti-TCRpV antibody molecule described herein), thereby expanding the immune cell population. In some embodiments, the expansion occurs in vivo or ex vivo (e.g., in vitro). In an aspect, provided herein is a method of evaluating a subject having a cancer, comprising acquiring a value of the status of a TCRPV molecule for the subject, wherein said value comprises a measure of the presence of, e.g., level or activity of, a TCRPV molecule in a sample from the subject, wherein the value of the status of a TCRpV molecule is higher, e.g., increased, in a sample from the subject compared to a reference value, e.g., a value from a healthy subject, e.g., a subject that does not have cancer. In another aspect, the disclosure provides a method of treating a subject having a cancer, the method comprising (i) acquiring a value of the status of a TCRPV molecule for the subject, wherein said value comprises a measure of the presence of, e.g., level or activity of, a TCRpV molecule in a sample from the subject, and (ii) responsive to said value, administering an effective amount of an anti- TCRPV antibody molecule described herein (e.g., a TCRpV agonist) to the subject, thereby treating the cancer. In some embodiments, the value is higher, e.g., increased, in a sample from the subject compared to a reference value, e.g., a value from a healthy subject, e.g., a subject that does not have cancer. In a related aspect, the disclosure provides a composition comprising an anti- TCRPV antibody molecule for use in the treatment of a subject having a cancer, comprising (i) acquiring a value of the status of a TCRPV molecule for the subject, wherein said value comprises a measure of the presence of, e.g., level or activity of, a TCRpV molecule in a sample from the subject, and (ii) responsive to said value, administering an effective amount of an anti- TCRPV antibody molecule described herein (e.g., a TCRpV agonist) to the subject. In an aspect, provided herein is method of evaluating a subject for the presence of a cancer, the method comprising: (i) acquiring a value of the status of one or more TCRPV molecules for the subject, e.g., in a biological sample from the subject, wherein said value comprises a measure of the presence of, e.g., level or activity of, a TCRpV molecule in a sample from the subject, and (ii) determining whether the value for the one or more TCRPV molecules is higher, e.g., increased, in a sample from the subject compared to a reference value, e.g., a value from a healthy subject, e.g., a subject that does not have cancer, wherein a value that is higher, e.g., increased, in the subject relative to the reference, e.g., healthy subject, is indicative of the presence of cancer in the subject. In another aspect, the disclosure provides, a method of treating a subject having cancer, the method comprising: (i) acquiring a value of the status of one or more TCRPV molecules for the subject, e.g., in a biological sample from the subject, wherein said value comprises a measure of the presence of, e.g., level or activity of, a TCRpV molecule in a sample from the subject; (ii) determining whether the value for the one or more TCRPV molecules is higher, e.g., increased, in a sample from the subject compared to a reference value, e.g., a value from a healthy subject, e.g., a subject that does not have cancer, and (iii) if a value that is higher, e.g., increased, in the subject relative to the reference value is determined, administering an effective amount of an anti- TCRPV antibody molecule, e.g., as described herein (e.g., a TCRPV agonist), to the subject, 32 thereby treating the cancer. In a related aspect, provided herein is a composition comprising anti- TCRPV antibody molecule for use in a method of treating a subject having a cancer, comprising (i) acquiring a value of the status of one or more TCRPV molecules for the subject, e.g., in a biological sample from the subject, wherein said value comprises a measure of the presence of, e.g., level or activity of, a TCRPV molecule in a sample from the subject; (ii) determining whether the value for the one or more TCRPV molecules is higher, e.g., increased, in a sample from the subject compared to a reference value, e.g., a value from a healthy subject, e.g., a subject that does not have cancer, and (iii) if a value that is higher, e.g., increased, in the subject relative to the reference value is determined, administering an effective amount of an anti- TCRPV antibody molecule, e.g., as described herein (e.g., a TCRpV agonist), to the subject. In some embodiments of any of the methods of treatment, or composition for use disclosed herein, the status is indicative of the subject having cancer, or a symptom thereof. In some embodiments of any of the methods of treatment or composition for use disclosed herein, the status is indicative of responsiveness to a therapy, e.g., a therapy comprising an anti-TCRpV antibody molecule, e.g., as described herein. In some embodiments of any of the methods of treatment or composition for use disclosed herein, the value of the status is determined, e.g., measured, by an assay described herein. In yet another aspect, provided herein is a method of treating a subject having a cancer, comprising administering to the subject an effective amount of an anti-TCRBV antibody molecule described herein, wherein the subject has a higher, e.g., increased, level or activity of one or more TCRBV molecules, e.g., as described herein, compared to a reference level or activity of one or more TCRBV molecules, e.g., in a healthy subject, e.g., a subject not having a cancer In an aspect, the disclosure provides, method of treating a subject having a cancer, comprising (i) isolating a biological sample from the subject; e.g., a peripheral blood sample, biopsy sample, or bone marrow sample; and (ii) acquiring a value of the status of one or more TCRPV molecules for the subject, e.g., in the biological sample from the subject, wherein said value comprises a measure of the 33 presence of, e.g., level or activity of, a TCRpV molecule in a sample from the subject compared to a reference value, e.g., a sample from a health subject, wherein a value that is higher, e.g., increased, in the subject relative to the reference, e.g., healthy subject, is indicative of the presence of cancer in the subject, (iii) contacting the biological sample with an anti-TCRPV antibody molecule, e.g., in vitro; and (iv) administering the biological sample or a portion thereof from step (iii) to the subject. In another aspect, provided herein is method of expanding a population of immune effector cells from a subject having a cancer, the method comprising: (i) isolating a biological sample comprising a population of immune effector cells from the subject; e.g., a peripheral blood sample, biopsy sample, or bone marrow sample; (ii) acquiring a value of the status of one or more TCRpV molecules for the subject, e.g., in the biological sample from the subject, wherein said value comprises a measure of the presence of, e.g., level or activity of, a TCRpV molecule in a sample from the subject compared to a reference value, e.g., a sample from a health subject, wherein a value that is higher, e.g., increased, in the subject relative to the reference, e.g., healthy subject, is indicative of the presence of cancer in the subject, and (iii) contacting the biological sample comprising a population of immune effector cells with an anti- TCRpV antibody molecule. In some embodiments, the method further comprises administering the population of immune effector cells contacted with the anti-TCRpV antibody molecule to the subject. In some embodiments, a method of expansion, or method of treatment, or composition for use disclosed herein comprises measuring T cell function (e.g., cytotoxic activity, cytokine secretion, or degranulation) in the population of immune effector cells, e.g., compared to a reference population, e.g., an otherwise similar population not contacted with the anti-TCRpV antibody molecule or a population of immune effector cells obtained from a healthy subject (e.g., a subject that does not have a cancer). In some embodiments of any of the methods or composition for use disclosed herein, the biological sample comprising the population of immune effector cells is contacted with an anti-TCRPV antibody molecule that binds to the one or more TCRPV molecules (e.g., the same TCRPV molecule) identified as being higher, e.g., increased, in the biological sample. In some embodiments of any of the methods or composition for use disclosed herein, the biological sample comprising the population of immune effector cells is contacted with an anti-TCRPV antibody molecule that does not bind to the one or more TCRPV molecules (e.g., a different TCRpV molecule) identified as being higher, e.g., increased, in the biological sample. 5 In another aspect, provided herein is a method of identifying one or more TCRpV molecules associated with a cancer, the method comprising: (i) acquiring a status for a plurality of TCRpV molecules in a biological sample from a first subject having the disease and in a biological sample from a second subject not having the 10 disease; and (ii) determining whether the level or activity of one or more of the TCRPV molecules is higher, e.g., increased, in the first subject relative to the second subject; thereby identifying one or more TCRPV molecules associated with the cancer. 15 In some embodiments of any of the methods or composition for use disclosed herein, the one or more of the TCRpV molecules comprises one or more, (e.g., all) of the following TCRPV subfamilies: (i) TCRp V6 subfamily comprising, e.g., one or more of TCRP V6-4*01, TCRP V6-4*02, TCRp V6-9*01, TCRp V6-8*01, TCRp V6-5*01, TCRp V6-6*02, TCRp V6-6*01, TCRp V6-2*01, TCRP V6-3*01 or TCRp V6-l*01; (ii) TCRP V10 subfamily comprising, e.g., one or more of TCRp V10-l*01, TCRP V10-1*02, TCRp V10-3*01 or TCRp V10-2*01; (iii) TCRp V5 subfamily comprising, e.g., one or more of TCRp V5-6*01, TCRp V5-4*01, or TCRp V5-8*01; (iv) TCRp V12 subfamily comprising e.g., one or more of TCRP V12-4*01, TCRP V12-3*01, or TCRp V12-5*01; (v) TCRp V7 subfamily comprising e.g., one or more of TCRp V7-7*01, TCRP V7-6*01, TCRp V7 -8*02, TCRp V7 -4*01, TCRp V7-2*02, TCRp V7-2*03, TCRp V7-2*01, TCRp V7-3*01, TCRp V7-9*03, or TCRp V7-9*01; (vi) TCRp Vil subfamily comprising e.g., one or more of TCRP VI 1-1*01, TCRP VI1-2*01 or TCRp VI 1-3*01; (vii) TCRP V14 subfamily comprising TCRP V14*01; (viii) TCRP VI6 subfamily comprising TCRP VI6*01; (ix) TCRp V18 subfamily comprising TCRP V18*01; (x) TCRp V9 subfamily comprising T e.g., one or more of CRP V9*01 or TCRp V9*02; 35 (xi) TCRP VI3 subfamily comprising TCRP VI3*01; (xii) TCRP V4 subfamily comprising e.g., one or more of e.g., one or more of TCRP V4-2*01, TCRp V4-3*01, or TCRp V4-l*01; (xiii) TCRP V3 subfamily comprising TCRP V3-l*01; (xiv) TCRP V2 subfamily comprising TCRP V2*01; (xv) TCRp VI5 subfamily comprising TCRP VI5*01; (xvi) TCRp V30 subfamily comprising e.g., one or more of TCRP V30*01, or TCRP V30*02; (xvii) TCRp V19 subfamily comprising e.g., one or more of TCRP V19*01, or TCRP V19*02; (xviii) TCRP V27 subfamily comprising TCRP V27*01; (xix) TCRP V28 subfamily comprising TCRP V28*01; (xx) TCRp V24 subfamily comprising TCRP V24-l*01; (xxi) TCRp V20 subfamily comprising e.g., one or more of TCRP V20-l*01, or TCRP V20-l*02; (xxii) TCRP V25 subfamily comprising TCRp V25-l*01; or (xxiii) TCRp V29 subfamily comprising TCRp V29-1 *01; (xxiv) TCRP V21 subfamily; (xxv) TCRp VI subfamily; (xxvi) TCRp VI7 subfamily; (xvii) TCRp V23 subfamily; or (xviii) TCRP V26 subfamily. In some embodiments of any of the methods or composition for use disclosed herein, the cancer is a solid tumor including but not limited to: melanoma, pancreatic (e.g., pancreatic adenocarcinoma) cancer, breast cancer, colorectal cancer (CRC), lung cancer (e.g., small or non-5 small cell lung cancer), skin cancer, ovarian cancer, or liver cancer. In some embodiments of any of the methods or composition for use disclosed herein, the cancer is a hematological cancer including, but not limited to: a B-cell or T cell malignancy, e.g., Hodgkin’s lymphoma, Non-Hodgkin’s lymphoma (e.g., B cell lymphoma, diffuse large B cell lymphoma (DLBCL), follicular lymphoma, chronic lymphocytic leukemia (B-CLL), mantle 10 cell lymphoma, marginal zone B-cell lymphoma, Burkitt lymphoma, lymphoplasmacytic lymphoma, hairy cell leukemia), acute myeloid leukemia (AML), chronic myeloid leukemia, myelodysplastic syndrome, multiple myeloma, and acute lymphocytic leukemia. In some embodiments of a method of expansion, or method of treatment, or composition for use disclosed herein, a higher, e.g., increased, level or activity of one or more TCRpV molecules in a subject, e.g., in a sample from a subject, is indicative of a bias, e.g., a preferential expansion, e.g., clonal expansion, of T cells expressing said one or more TCRPV molecules in the subject. In some embodiments, a subject having a cancer, e.g., as disclosed herein, has a higher, e.g., increased, level or activity of one or more TCRpV molecules associated with the cancer. In some embodiments, the TCRpV molecule is associated with, e.g., recognizes, a cancer antigen, e.g., a cancer associated antigen or a neoantigen. In some embodiments of any of the methods or composition for use disclosed herein, the subject has B-CLL. In some embodiments, a subject having B-CLL has a higher, e.g., increased, level or activity of one or more TCRPV molecules, e.g., one or more TCRpV molecules comprising: (i) TCRP V6 subfamily comprising, e.g., TCRP V6-4*01, TCRp V6-4*02, TCRp V6-9*01, TCRp V6-8*01, TCRp V6-5*01, TCRp V6-6*02, TCRp V6-6*01, TCRp V6-2*01, TCRp V6-3*01 or TCRp V6-l*01; (ii) TCRp V5 subfamily comprising TCRp V5-6*01, TCRp V5-4*01, or TCRp V5-8*01; (iii) TCRp V3 subfamily comprising TCRp V3-1 *01; (iv) TCRP V2 subfamily comprising TCRp V2*01; or (v) TCRP V19 subfamily comprising TCRp VI9*01, or TCRp VI9*02. In some embodiments, a subject having B-CLL has a higher, e.g., increased, level or activity of a TCRP V6 subfamily comprising, e.g., TCRP V6-4*01, TCRP V6-4*02, TCRP V6-9*01, TCRp V6-8*01, TCRp V6-5*01, TCRp V6-6*02, TCRp V6-6*01, TCRp V6-2*0L TCRp V6-3*01 or TCRp V6-l*01. In some embodiments, the subject is administered an anti-TCRpV molecule (e.g., an agonistic anti- TCRpV molecule as described herein) that binds to one or more members of the TCRP V6 subfamily. In some embodiments, administration of the an anti-TCRPV molecule results in expansion of immune cells expressing one or more members of the TCRp V6 subfamily. In some embodiments, a subject having B-CLL has a higher, e.g., increased, level or activity of a TCRP V5 subfamily comprising TCRP V5-6*01, TCR0 V5-4*01, or TCRP V5-8*01. In some embodiments, the subject is administered an anti-TCRpV molecule (e.g., an agonistic anti- TCRpV molecule as described herein) that binds to one or more members of the TCRP V5 subfamily. In some embodiments, administration of the an anti-TCRpV molecule results in expansion of immune cells expressing one or more members of the TCRP V5 subfamily. In some embodiments, a subject having B-CLL has a higher, e.g., increased, level or activity of a TCRP V3 subfamily comprising TCRP V3-l*01. In some embodiments, the subject is administered an anti-TCRpV molecule (e.g., an agonistic anti- TCRPV molecule as described herein) that binds to one or more members of the TCRP V3 subfamily. In some embodiments, administration of the an anti-TCRpV molecule results in expansion of immune cells expressing one or more members of the TCRP V3 subfamily. In some embodiments, a subject having B-CLL has a higher, e.g., increased, level or activity of a TCRP V2 subfamily comprising TCRP V2*01. In some embodiments, the subject is administered an anti-TCRpV molecule (e.g., an agonistic anti- TCRPV molecule as described herein) that binds to one or more members of the TCRP V2 subfamily. In some embodiments, administration of the an anti-TCRpV molecule results in expansion of immune cells expressing one or more members of the TCRp V2 subfamily. In some embodiments, a subject having B-CLL has a higher, e.g., increased, level or activity of a TCRP VI9 subfamily comprising TCRP VI 9*01, or TCRP VI 9*02. In some embodiments, the subject is administered an anti-TCRpV molecule (e.g., an agonistic anti-TCRBV molecule as described herein) that binds to one or more members of the TCRP V19 subfamily. In some embodiments, administration of the an anti-TCRpV molecule results in expansion of immune cells expressing one or more members of the TCRP V19 subfamily. In some embodiments of any of the methods or composition for use disclosed herein, the subject has melanoma. In some embodiments, a subject having melanoma has a higher, e.g., increased, level or activity of one or more TCRPV molecules, e.g., one or more TCRPV molecules comprising the TCRP V6 subfamily comprising, e.g., TCRP V6-4*01, TCRP V6-4*02, TCRp V6-9*01, TCRp V6-8*01, TCRp V6-5*01, TCRp V6-6*02, TCRp V6-6*01, TCRp V6-2*01, TCRP V6-3*01 or TCRP V6-l*01. In some embodiments, the subject is administered an anti-TCRpV molecule (e.g., an agonistic anti-TCRpV molecule as described herein) that binds to one or more members of the TCRp V6 subfamily. In some embodiments, administration of the an anti-TCRpV molecule results in expansion of immune cells expressing one or more members of the TCRP V6 subfamily. In some embodiments of any of the methods or composition for use disclosed herein, the subject has DLBCL. In some embodiments, a subject having melanoma has a higher, e.g., increased, level or activity of one or more TCRpV molecules, e.g., one or more TCRPV molecules comprising: (i) TCRp VI3 subfamily comprising TCRP VI3 *01; (ii) TCRp V3 subfamily comprising TCRP V3-l*01; or (iii) TCRP V23 subfamily. In some embodiments, a subject having DLBCL has a higher, e.g., increased, level or activity of a TCRP ¥13 subfamily comprising TCRP VI3 *01. In some embodiments, the subject is administered an anti-TCRpV molecule (e.g., an agonistic anti- TCRPV molecule as described herein) that binds to one or more members of the TCRP VI3 subfamily. In some embodiments, administration of the an anti-TCRpV molecule results in expansion of immune cells expressing one or more members of the TCRP VI3 subfamily. In some embodiments, a subject having DLBCL has a higher, e.g., increased, level or activity of a TCRP V3 subfamily comprising TCRP V3-l*01. In some embodiments, the subject is administered an anti-TCRpV molecule (e.g., an agonistic anti- TCRPV molecule as described herein) that binds to one or more members of the TCRP V3 subfamily. In some embodiments, administration of the an anti-TCRpV molecule results in expansion of immune cells expressing one or more members of the TCRp V3 subfamily. In some embodiments, a subject having DLBCL has a higher, e.g., increased, level or activity of a TCRP V23 subfamily. In some embodiments, the subject is administered an anti-TCRPV molecule (e.g., an agonistic anti- TCRpV molecule as described herein) that binds to one or more members of the TCRp V23 subfamily. In some embodiments, administration of the an anti-TCRpV molecule results in expansion of immune cells expressing one or more members of the TCRP V23 subfamily. In some embodiments of any of the methods or composition for use disclosed herein, the subject has CRC. In some embodiments, a subject having melanoma has a higher, e.g., increased, level or activity of one or more TCRPV molecules, e.g., one or more TCRPV molecules comprising: (i) TCRp V19 subfamily comprising TCRp V19*01, or TCRp V19*02; (ii) TCRp V12 subfamily comprising TCRp ¥12-4*01, TCRp V12-3*01, or TCRp ¥12-5*01; (iii) TCRP ¥16 subfamily comprising TCRP ¥16*01; or (iv) TCRP ¥21 subfamily. In some embodiments, a subject having CRC has a higher, e.g., increased, level or activity of a TCRp ¥19 subfamily comprising TCRP ¥19*01, or TCRp ¥19*02. In some embodiments, the subject is administered an anti-TCRpV molecule (e.g., an agonistic anti-TCRp¥ molecule as described herein) that binds to one or more members of the TCRp V19 subfamily. In some embodiments, administration of the an anti-TCRp¥ molecule results in expansion of immune cells expressing one or more members of the TCRP ¥19 subfamily. In some embodiments, a subject having CRC has a higher, e.g., increased, level or activity of a TCRp ¥12 subfamily comprising TCRp ¥12-4*01, TCRp ¥12-3*01, or TCRp ¥12-5*01. In some embodiments, the subject is administered an anti-TCRp¥ molecule (e.g., an agonistic anti- TCRpV molecule as described herein) that binds to one or more members of the 39 TCRP V12 subfamily. In some embodiments, administration of the an anti-TCRpv molecule results in expansion of immune cells expressing one or more members of the TCRP V12 subfamily. In some embodiments, a subject having CRC has a higher, e.g., increased, level or activity of a TCRP V16 subfamily comprising TCRp V16*01. In some embodiments, the subject is administered an anti-TCRpv molecule (e.g., an agonistic anti- TCRpV molecule as described herein) that binds to one or more members of the TCRP V16 subfamily. In some embodiments, administration of the an anti-TCRpV molecule results in expansion of immune cells expressing one or more members of the TCRP VI6 subfamily. In some embodiments, a subject having CRC has a higher, e.g., increased, level or activity of a TCRp V21 subfamily. In some embodiments, the subject is administered an anti-TCRpV molecule (e.g, an agonistic anti- TCRPV molecule as described herein) that binds to one or more members of the TCRP V21 subfamily. In some embodiments, administration of the an anti-TCRpV molecule results in expansion of immune cells expressing one or more members of the TCRP V21 subfamily. Alternatively or in combination with any of the embodiments disclosed herein, provided herein is an anti-TCRpV antibody molecule which: (i) binds specifically to an epitope on TCRPV, e.g., the same or similar epitope as the epitope recognized by an anti-TCRpV antibody molecule as described herein, e.g., a second anti-TCRpV antibody molecule; (ii) shows the same or similar binding affinity or specificity, or both, as an anti-TCRpV antibody molecule as described herein, e.g., a second anti-TCRpV antibody molecule; (iii) inhibits, e.g., competitively inhibits, the binding of an anti-TCRpV antibody molecule as described herein, e.g., a second anti-TCRpV antibody molecule; (iv) binds the same or an overlapping epitope with an anti-TCRpV antibody molecule as described herein, e.g., a second anti-TCRpv antibody molecule; or (v) competes for binding, and / or binds the same epitope, with an anti-TCRpV antibody molecule as described herein, e.g., a second anti-TCRpv antibody molecule, In some embodiments, the second anti-TCRpv antibody molecule comprises an antigen binding domain chosen from Table 1 or Table 2, or a sequence substantially identical thereto. In some embodiments, the second anti-TCRpv antibody molecule comprises an antigen binding domain, comprising: a heavy chain complementarity determining region 1 (HC CDR1), a heavy chain complementarity determining region 2 (HC CDR2) and / or a heavy chain complementarity 40 determining region 3 (HC CDR3) of SEQ ID NO: 1 or SEQ ID NO: 9; and / or a light chain complementarity determining region 1 (LC CDR1), a light chain complementarity determining region 2 (LC CDR2), and / or a light chain complementarity determining region 3 (LC CDR3) of SEQ ID NO: 2, SEQ ID NO: 10 or SEQ ID NO: 11. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises an antigen binding domain comprising: (i) a heavy chain complementarity determining region 1 (HC CDR1), a heavy chain complementarity determining region 2 (HC CDR2) and / or a heavy chain complementarity determining region 3 (HC CDR3) of SEQ ID NO: 1 or SEQ ID NO: 9, or a sequence disclosed in Table 1; or (ii) a light chain complementarity determining region 1 (LC CDR1), a light chain complementarity determining region 2 (LC CDR2), and / or a light chain complementarity determining region 3 (LC CDR3) of SEQ ID NO: 2, SEQ ID NO: 10 or SEQ ID NO: 11, or a sequence disclosed in Table 1. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises an antigen binding domain comprising a light chain variable region (VL) comprising one, two or all (e.g., three) of a LC CDR1, a LC CDR2 and a LC CDR3 of SEQ ID NO: 2, SEQ ID NO: 10 or SEQ ID NO: 11. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a heavy chain variable region (VH) comprising one, two or all (e.g., three) of a HC CDR1, a HC CDR2 and a HC CDR3 of SEQ ID NO: 1 or SEQ ID NO: 9. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises an antigen binding domain comprising: (i) a VL comprising: a LC CDR1 amino acid sequence of SEQ ID NO: 6 (or an amino acid sequence with not more than 1, 2, 3 or 4 modifications, e.g., substitutions, additions or deletions thereof), a LC CDR2 amino acid sequence of SEQ ID NO:7 (or an amino acid sequence with not more than 1, 2, 3 or 4 modifications, e.g., substitutions, additions or deletions thereof), and / or a LC CDR3 amino acid sequence of SEQ ID NO:8 (or an amino acid sequence with not more than 1, 2, 3 or 4 modifications, e.g., substitutions, additions or deletions thereof); and / or (ii) a VH comprising: a HC CDR1 amino acid sequence of SEQ ID NO: 3 (or an amino acid sequence with not more than 1, 2, 3 or 4 modifications, e.g., substitutions, additions or 41 deletions thereof), a HC CDR2 amino acid sequence of SEQ ID NO:4 (or an amino acid sequence with not more than 1, 2, 3 or 4 modifications, e.g., substitutions, additions or deletions thereof), and / or a HC CDR3 amino acid sequence of SEQ ID NO:5 (or an amino acid sequence with not more than 1, 2, 3 or 4 modifications, e.g., substitutions, additions or deletions thereof). In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises an antigen binding domain comprising: a variable heavy chain (VH) of SEQ ID NO: 9 or SEQ ID NO: 1312, or a sequence having at least about 75%, 80%, 85%, 90%, 95%, or 99% sequence identity thereto; and / or a variable light chain (VL) of SEQ ID NO: 10 or SEQ ID NO: 11 or SEQ ID NO: 1314, or a sequence having at least about 75%, 80%, 85%, 90%, 95%, or 99% sequence identity thereto. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises an antigen binding domain comprising the VH amino acid sequence of SEQ ID NO: 9 and the VL amino acid sequence of SEQ ID NO: 10. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising the VH amino acid sequence of SEQ ID NO: 9 and the VL amino acid sequence of SEQ ID NO: 11. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises an antigen binding domain comprising the VH amino acid sequence of SEQ ID NO: 1312 and the VL amino acid sequence of SEQ ID NO: 1314. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising the amino acid sequence of SEQ ID NO: 1337, or a sequence with at least 85%, 90%, 95%, 96%, 97%, 98% or 99% identity thereto. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises an antigen binding domain comprising the amino acid sequence of SEQ ID NO: 1500, or a sequence with at least 85%, 90%, 95%, 96%, 97%, 98% or 99% identity thereto. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises a heavy chain comprising a framework region, e.g., framework region 3 (FR3), comprising one or both of: (i) a Threonine at position 73, e.g., a substitution at position 73 according to Kabat numbering, e.g., a Glutamic Acid to Threonine substitution; or (ii) a Glycine at position, e.g., a substitution at position 94 according to Kabat numbering, e.g., a Arginine to Glycine substitution. In some embodiments, the substitution is relative to a human germline heavy chain framework region sequence. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises a light chain comprising a framework region, e.g., framework region 1 (FR1), comprising a Phenylalanine at position 10, e.g., a substitution at position 10 according to Kabat numbering, e.g., a Serine to Phenyalanine substitution. In some embodiments, the substitution is relative to a human germline light chain framework region sequence. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRpV antibody molecule comprises a light chain comprising a framework region, e.g., framework region 2 (FR2), comprising one or both of: (i) a Histidine at position 36, e.g., a substitution at position 36 according to Kabat numbering, e.g., a Tyrosine to Histidine substitution; or (ii) an Alanine at position 46, e.g., a substitution at position 46 according to Kabat numbering, e.g., a Arginine to Alanine substitution. In some embodiments, the substitution is relative to a human germline light chain framework region sequence. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises a light chain comprising a framework region, e.g., framework region 3 (FR3), comprising a Phenylalanine at position 87, e.g., a substitution at position 87 according to Kabat numbering, e.g., a Tyrosine to Phenyalanine substitution. In some embodiments, the substitution is relative to a human germline light chain framework region sequence. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRpV antibody molecule binds to TCRp ¥6, e.g., TCRp ¥6-4*01, TCRp V6-4*02, TCRp ¥6-9*01, TCRp ¥6-8*01, TCRp ¥6-5*01, TCRp V6-6*02, TCRp ¥6-6*01, TCRp ¥6-2*01, TCRp V6-3*01 or TCRp ¥6-1*01. In some embodiments the anti-TCRp¥ antibody molecule binds to TCRp ¥6-5*01. In some embodiments, TCRp ¥6, e.g., TCRp ¥6-4*01, TCRp ¥6-4*02, TCRp ¥6-9*01, TCRp ¥6-8*01, TCRp ¥6-5*01, TCRp ¥6-6*02, TCRp ¥6-6*01, TCRp ¥6-2*01, TCRp ¥6-3*01 or TCRP ¥6-1*01, is recognized, e.g., bound, by SEQ ID NO: 1 and / or SEQ ID NO: 2. In some embodiments, TCRp ¥6, e.g., TCRp ¥6-4*01, TCRp ¥6-4*02, TCRp ¥6-9*01, TCRp ¥6-8*01, TCRP ¥6-5*01, TCRp ¥6-6*02, TCRp ¥6-6*01, TCRp ¥6-2*01, TCRp ¥6-3*01 or TCRP ¥6-1*01, is recognized, e.g., bound, by SEQ ID NO: 9 and / or SEQ ID NO: 10. In some embodiments, TCRp ¥6, e.g., TCRp ¥6-4*01, TCRp ¥6-4*02, TCRp ¥6-9*01, TCRp ¥6-8*01, TCRp ¥6-5*01, TCRp ¥6-6*02, TCRp ¥6-6*01, TCRp ¥6-2*01, TCRp ¥6-3*01 or TCRP ¥6-1*01, is recognized, e.g., bound, by SEQ ID NO: 9 and / or SEQ ID NO: 11. In some 43 embodiments, TCRP V6-5*01 is recognized, e.g.. bound by SEQ ID NO: 9 and / or SEQ ID NO: 10, or a sequence having at least about 75%, 80%, 85%, 90%, 95%, or 99% sequence identity thereto. In some embodiments, TCRP V6-5*01 is recognized, e.g., bound by SEQ ID NO: 9 and / or SEQ ID NO: 11, or a sequence having at least about 75%, 80%, 85%, 90%, 95%, or 99% sequence identity thereto. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises an antigen binding domain comprising: (i) a heavy chain complementarity determining region (HC CDR1), a HC CDR2 and / or a HC CDR3 of SEQ ID NO: 15, SEQ ID NO: 23, SEQ ID NO: 24 or SEQ ID NO: 25, or a sequence disclosed in Table 2; and / or (ii) a light chain complementarity determining region 1 (LC CDR1), a LC CDR2, and / or a LC CDR3 of SEQ ID NO: 16, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 29 or SEQ ID NO:30, or a sequence disclosed in Table 2. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a light chain variable region (VL) comprising one, two or all of a LC CDR1, a LC CDR2 and a LC CDR3 of SEQ ID NO: 16, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 29 or SEQ ID NO:30. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a heavy chain variable region (VH) comprising one, two or all of a HC CDR1, a HC CDR2 and a HC CDR3 of SEQ ID NO: 15, SEQ ID NO: 23, SEQ ID NO: 24 or SEQ ID NO: 25. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises an antigen binding domain comprising: (i) a VL comprising: a LC CDR1 amino acid sequence of SEQ ID NO: 20 (or an amino acid sequence with not more than 1, 2, 3 or 4 modifications, e.g., substitutions, additions or deletions thereof), a LC CDR2 amino acid sequence of SEQ ID NO:21 (or an amino acid sequence with not more than 1, 2, 3 or 4 modifications, e.g., substitutions, additions or deletions thereof), and / or a LC CDR3 amino acid sequence of SEQ ID NO:22 (or an amino acid sequence with not more than 1, 2, 3 or 4 modifications, e.g., substitutions, additions or deletions thereof); and / or (ii) a VH comprising: a HC CDR1 amino acid sequence of SEQ ID NO: 17 (or an amino acid sequence with not more than 1, 2, 3 or 4 modifications, e.g., substitutions, additions or deletions thereof), a HC CDR2 amino acid sequence of SEQ ID NO: 18 (or an amino acid 44 sequence with not more than 1, 2, 3 or 4 modifications, e.g., substitutions, additions or deletions thereof), and / or a HC CDR3 amino acid sequence of SEQ ID NO: 19 (or an amino acid sequence with not more than 1, 2, 3 or 4 modifications, e.g., substitutions, additions or deletions thereof). In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises an antigen binding domain comprising: a variable heavy chain (VH) of SEQ ID NO: 23, SEQ ID NO: 24 or SEQ ID NO: 25, or a sequence having at least about 75%, 80%, 85%, 90%, 95%, or 99% sequence identity thereto; and / or a variable light chain (VL) of SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 29 or SEQ ID NO:30, or a sequence having at least about 75%, 80%, 85%, 90%, 95%, or 99% sequence identity thereto. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises a light chain comprising a framework region, e.g., framework region 1 (FR1), comprising one, two or all (e.g., three) of: (i) an Aspartic Acid at position 1, e.g., a substitution at position 1 according to Kabat numbering, e.g., a Alanine to Aspartic Acid substitution; or (ii) an Asparagine at position 2, e.g., a substitution at position 2 according to Kabat numbering, e.g., a Isoleucine to Asparagine substitution, a Serine to Asparagine substitution, or a Tyrosine to Asparagine substitution; or (iii) a Leucine at position 4, e.g., a substitution at position 4 according to Kabat numbering, e.g., a Methionine to Leucine substitution. In some embodiments, the substitution is relative to a human germline light chain framework region sequence. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises a light chain comprising a framework region, e.g., framework region 3 (FR3), comprising one, two or all (e.g., three) of: (i) a Glycine as position 66, e.g., a substitution at position 66 according to Kabat numbering, e.g., a Lysine to Glycine substitution, or a Serine to Glycine substitution; or (ii) an Asparagine at position 69, e.g., a substitution at position 69 according to Kabat numbering, e.g., a Threonine to Asparagine substitution; or (iii) a Tyrosine at position 71, e.g., a substitution at position 71 according to Kabat numbering, e.g., a Phenylalanine to Tyrosine substitution, or an Alanine to Tyrosine substitution. In some embodiments, the substitution is relative to a human germline light chain framework region sequence. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRpV antibody molecule binds to TCRp V12, e.g, TCRp V12-4*01, TCRp V12-3*01, or TCRP V12-5*01. In some embodiments the anti-TCRpV antibody molecule binds to TCRp V12-4*01 or TCRp V12-3*01. In some embodiments, TCRP V12, e.g., TCRP V12-4*01, TCRP V12-3*01, or TCRp V12-5*01 is recognized, e.g., bound, by SEQ ID NO: 15 and / or SEQ ID NO: 16. In some embodiments, TCRp V12, e.g., TCRp V12-4*01, TCRp V12-3*01, or TCRp V12-5*01, is recognized, e.g., bound, by any one of SEQ ID NOs 23-25, and / or any one of SEQ ID NO: 26-30, or an amino acid sequence having at least about 75%, 80%, 85%, 90%, 95%, or 99% sequence identity thereto. In some embodiments TCRp VI2-4*01 is recognized, e.g., bound, by any one of SEQ ID NOs 23-25, and / or any one of SEQ ID NO: 26-30, or an amino acid sequence having at least about 75%, 80%, 85%, 90%, 95%, or 99% sequence identity thereto. In some embodiments TCRP V12-3*01 is recognized, e.g., bound, by any one of SEQ ID NOs 23-25, and / or any one of SEQ ID NO: 26-30, or an amino acid sequence having at least about 75%, 80%, 85%, 90%, 95%, or 99% sequence identity thereto. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises the anti-TCRpV antibody molecule comprises an antigen binding domain comprising a single chain Fv (scFv) or a Fab. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises binds to a conformational or a linear epitope on the T cell. In some embodiments of any of the compositions or methods disclosed herein, the tumor comprises an antigen, e.g., a tumor antigen, e.g., a tumor associated antigen or a neoantigen. In some embodiments, the anti-TCRpV antibody molecule recognize, e.g., bind to, the tumor antigen. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule is a full antibody (e.g., an antibody that includes at least one, and preferably two, complete heavy chains, and at least one, and preferably two, complete light chains), or an antigen-binding fragment (e.g., a Fab, F(ab')v Fv, a single chain Fv fragment, a single domain antibody, a diabody (dAb), a bivalent antibody, or bispecific antibody or fragment thereof, a single domain variant thereof, a camelid antibody, or a rat-derived VH. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises the anti-TCRpV antibody molecule comprises one or more heavy chain constant regions chosen from IgG 1, IgG2, IgG3, IgGAl, IgGA2, IgM, IgJ or IgG4, or a fragment thereof, e.g., as disclosed in Table 3. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises a heavy chain constant region of an IgM or a fragment thereof, optionally wherein the IgM heavy chain constant region comprises the sequence of SEQ ID NO: 73, or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRpV antibody molecule comprising an IgM constant region, further comprises a heavy chain constant region of an IgJ or a fragment thereof, optionally wherein the IgJ heavy chain constant region comprises the sequence of SEQ ID NO: 76 or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRpV antibody molecule comprises a heavy chain constant region of an IgJ or a fragment thereof, optionally wherein the IgJ heavy chain constant region comprises the sequence of SEQ ID NO: 76 or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises a heavy chain constant region of an IgGAl, or a fragment thereof, optionally wherein the IgGAl heavy chain constant region comprises the sequence of SEQ ID NO: 74, or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises a heavy chain constant region of an IgGA2, or a fragment thereof, optionally wherein the IgGA2 heavy chain constant region comprises a sequence listed in Table 3, e.g., SEQ ID NO: 75, or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto. In some embodiments of any of the compositions or methods disclosed herein, binding of the anti-TCRpV antibody molecule to a TCRPV region results in a cytokine profile, e.g., a cytokine secretion profile, (e.g., comprising one or more cytokines and / or one or more chemokines), that differs from that of a T cell engager that binds to a receptor or molecule other than a TCRpV region (“a non-TCRpV-binding T cell engager"). In some embodiments, the cytokine profile, e.g., cytokine secretion profile, comprises the level and / or activity of one or more cytokines and / or one or more chemokines (e.g., as described herein). In an embodiment, a cytokine profile, e.g., a cytokine secretion profile, comprises the level and / or activity of one or more of: IL-2 (e.g., full length, a variant, or a fragment thereof); IL-1 beta (e.g., full length, a variant, or a fragment thereof); IL-6 (e.g., full length, a variant, or a fragment thereof); TNFa (e.g., full length, a variant, or a fragment thereof); IFNg (e.g., full length, a variant, or a fragment thereof) IL-10 (e.g., full length, a 47 variant, or a fragment thereof); IL-4 (e.g., full length, a variant, or a fragment thereof); TNF alpha (e.g., full length, a variant, or a fragment thereof);IL-12p70 (e.g., full length, a variant, or a fragment thereof); IL-13 (e.g., full length, a variant, or a fragment thereof); IL-8 (e.g., full length, a variant, or a fragment thereof); Eotaxin (e.g., full length, a variant, or a fragment thereof); Eotaxin-3 (e.g., full length, a variant, or a fragment thereof); IL-8 (HA) (e.g., full length, a variant, or a fragment thereof); IP-10 (e.g., full length, a variant, or a fragment thereof); MCP-1 (e.g., full length, a variant, or a fragment thereof); MCP-4 (e.g., full length, a variant, or a fragment thereof); MDC (e.g., full length, a variant, or a fragment thereof); MIP-la (e.g., full length, a variant, or a fragment thereof); MIP-lb (e.g., full length, a variant, or a fragment thereof); TARC (e.g., full length, a variant, or a fragment thereof); GM-CSF (e.g., full length, a variant, or a fragment thereof); IL-12 23p40 (e.g., full length, a variant, or a fragment thereof); IL-15 (e.g., full length, a variant, or a fragment thereof); IL-16 (e.g., full length, a variant, or a fragment thereof); IL-17a (e.g., full length, a variant, or a fragment thereof); IL-la (e.g., full length, a variant, or a fragment thereof); IL-5 (e.g., full length, a variant, or a fragment thereof); IL-7 (e.g., full length, a variant, or a fragment thereof); TNF-beta (e.g., full length, a variant, or a fragment thereof); or VEGF (e.g., full length, a variant, or a fragment thereof). In some embodiments, the cytokine profile, e.g., cytokine secretion profile, comprises one, two, three, four, five, six, seven, or all of the following: (i) increased level, e.g., expression level, and / or activity of IL-2; (ii) reduced level, e.g., expression level, and / or activity of IL-1P; (iii) reduced level, e.g., expression level, and / or activity of IL-6; (iv) reduced level, e.g., expression level, and / or activity of TNFa; (v) reduced level, e.g., expression level, and / or activity of IL-10; (vi) a delay, e.g., at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 or more hours delay, in increased level, e.g., expression level, and / or activity of IL-2; (vii) a delay, e.g., at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 hours delay, in increased level, e.g., expression level, and / or activity of IFNg; or (viii) increased level, e.g., expression level, and / or activity of IL-15, e.g., wherein (i)-(viii) are relative to the cytokine profile, e.g., cytokine secretion profile, of the non-TCRpV-binding T cell engager. In some embodiments, binding of the anti-TCRBV antibody to a TCRPV region results in reduced cytokine storm, e.g., reduced cytokine release syndrome (CRS) and / or neurotoxicity (NT), as measured by an assay of Example 3, e.g., relative to the cytokine storm induced by the non-TCRpV-binding T cell engager. In some embodiments, binding of the anti-TCRBV antibody to a TCRPV region results in one, two, three or all of: (ix) reduced T cell proliferation kinetics; (x) cell killing, e.g., target cell killing, e.g. cancer cell killing, e.g., as measured by an assay of Example 4; (xi) increased Natural Killer (NK) cell proliferation, e.g., expansion; or (xii) expansion, e.g., at least about 1.1-10 fold expansion (e.g., at least about 1.1, 1.2, 1.3, 1.4, 1.5, 2, 3, 4, 5, 6, 7, 8, 9, or 10 fold expansion), of a population of T cells having a memory-like phenotype, e.g., wherein (ix)-(xii) are relative to the non-TCRpV-binding T cell engager. In some embodiments, an anti-TCRpV antibody molecule disclosed herein recognizes (e.g., binds to), a structurally conserved domain on the TCRpV protein (e.g., as denoted by the circled area in FIG. 24A). In some embodiments, an anti-TCRpV antibody molecule disclosed herein does not recognize, e.g., bind to, an interface of a TCRpV:TCRalpha complex. In some embodiments, an anti-TCRpV antibody molecule disclosed herein does not recognize, e.g., bind to, a constant region of a TCRPV protein. An exemplary antibody that binds to a constant region of a TCRBV region is JOVI. 1 as described in Viney et al., (Hybridoma. 1992 Dec;l 1(6):701-13). In some embodiments, an anti-TCRpV antibody molecule disclosed herein does not recognize, e.g., bind to, one or more (e.g., all) of a complementarity determining region (e.g., CDR1, CDR2 and / or CDR3) of a TCRPV protein. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRpV antibody molecule comprises a light chain constant region chosen from the light chain constant regions of kappa or lambda, or a fragment thereof, e.g., as disclosed in Table 3. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises a light chain constant region of a kappa chain, or a fragment thereof, optionally wherein the kappa chain constant region comprises the sequence of SEQ ID NO: 39, or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises: (i) one or more heavy chain constant regions comprising a heavy chain constant region chosen from IgGl, IgG2, IgG3, IgGAl, IgGA2, IgG4, IgJ, IgM, IgD, or IgE, or a fragment thereof, e.g, as described in Table 3; and (ii) a light chain constant region comprising a light chain constant region chosen from the light chain constant regions of kappa or lambda, or a fragment thereof, e.g., as described in Table 3. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRpV antibody molecule comprises or a cell comprising an anti- TCRpV antibody molecule comprises: (i) a heavy chain comprising a variable region (VH), e.g., a VH of an antibody disclosed herein; and / or one or more heavy chain constant regions, e.g., as disclosed herein; and / or (ii) a light chain comprising a variable light (VL), e.g., a VL of an antibody disclosed herein; and / or one or more light chain constant regions, e.g., as disclosed herein. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises, or a cell comprising an anti- TCRPV antibody molecule comprises: (i) a heavy chain comprising a heavy chain constant region comprising: (a) an IgM heavy chain constant region or a fragment thereof, comprising the sequence of SEQ ID NO: 73, or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto; (b) an IgGAl heavy chain constant region or a fragment thereof, comprising the sequence of SEQ ID NO: 74, or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto; or (c) an IgGA2 heavy chain constant region or a fragment thereof, comprising the sequence of SEQ ID NO: 75, or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto; and (ii) a light chain comprising a light chain constant region comprising a kappa chain constant region comprising the sequence of SEQ ID NO: 39, or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto, optionally wherein, the anti-TCRpV antibody molecule further comprises an IgJ heavy chain constant region or a fragment thereof, wherein the IgJ heavy chain constant region comprises the sequence of SEQ ID NO: 76 or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto. In some embodiments of any of the compositions or methods disclosed herein, the anti-TCRPV antibody molecule comprises, or a cell comprising an anti- TCRpV antibody molecule comprises: (i) a heavy chain comprising: a VH chosen from a VH of Tables 1-2 or 10-13, or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto; and a heavy chain constant region comprising: (a) an IgM heavy chain constant region or a fragment thereof, comprising the sequence of SEQ ID NO: 73, or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto; (b) an IgGAl heavy chain constant region or a fragment thereof, comprising the sequence of SEQ ID NO: 74, or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto; or (c) an IgGA2 heavy chain constant region or a fragment thereof, comprising the sequence of SEQ ID NO: 75, or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto; and (ii) a light chain comprising: a VL chosen from a VL of Tables 1-2 or 10-13, or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto; and a light chain constant region comprising a kappa chain constant region comprising the sequence of SEQ ID NO: 39, or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto, optionally wherein, the anti-TCRpV antibody molecule further comprises an IgJ heavy chain constant region or a fragment thereof, wherein the IgJ heavy chain constant region comprises the sequence of SEQ ID NO: 76 or a sequence with at least 85%, 90%, 95%, or 99% sequence identity thereto. In some embodiments of any of the methods disclosed herein, the anti-TCRpV antibody molecule binds to one or more (e.g., all) of the following TCRpV subfamilies: (i) TCRP V6 subfamily comprising, e.g., one or more of TCRP V6-4*01, TCRp V6-4*02, TCRp V6-9*01, TCRp V6-8*01, TCRp V6-5*01, TCRp ¥6-6*02, TCRp V6-6*01, TCRp V6-2*01, TCRP V6-3*01 or TCRp V6-l*01; (ii) TCRp VI0 subfamily comprising, e.g., one or more of TCRP VI0-1 *01, TCRP VI0-1*02, TCRp V10-3*01 or TCRp V10-2*01; (iii) TCRp ¥5 subfamily comprising, e.g., one or more of TCRP ¥5-6*01, TCRP ¥5-4*01, or TCRp ¥5-8*01; (iv) TCRp ¥12 subfamily comprising e.g., one or more of TCRP ¥12-4*01, TCRp ¥12-3*01, or TCRp ¥12-5*01; (v) TCRP ¥7 subfamily comprising e.g., one or more of TCRP ¥7-7*01, TCRP ¥7-6*01, TCRp ¥7 -8*02, TCRp ¥7 -4*01, TCRp ¥7-2*02, TCRp ¥7-2*03, TCRp ¥7-2*01, TCRp ¥7-3*01, TCRp ¥7-9*03, or TCRp ¥7-9*01; (vi) TCRp ¥11 subfamily comprising e.g., one or more of TCRp ¥11-1*01, TCRp ¥11-2*01 or TCRp ¥11-3*01; (vii) TCRp ¥14 subfamily comprising TCRp ¥14*01; (viii) TCRp ¥16 subfamily comprising TCRp ¥16*01; (ix) TCRp ¥18 subfamily comprising TCRp ¥18*01; (x) TCRp ¥9 subfamily comprising T e.g., one or more of CRP ¥9*01 or TCRP ¥9*02; (xi) TCRp ¥13 subfamily comprising TCRP ¥13*01; (xii) TCRP ¥4 subfamily comprising e.g., one or more of e.g., one or more of TCRp ¥4-2*01, TCRp ¥4-3*01, or TCRp ¥4-1*01; (xiii) TCRP ¥3 subfamily comprising TCRp ¥3-1*01; (xiv) TCRp ¥2 subfamily comprising TCRP ¥2*01; (xv) TCRP ¥15 subfamily comprising TCRP ¥15*01; (xvi) TCRP ¥30 subfamily comprising e.g., one or more of TCRP ¥30*01, or TCRp ¥30*02; (xvii) TCRP ¥19 subfamily comprising e.g., one or more of TCRp ¥19*01, or TCRp ¥19*02; (xviii) TCRP ¥27 subfamily comprising TCRP ¥27*01; (xix) TCRP ¥28 subfamily comprising TCRP ¥28*01; (xx) TCRp ¥24 subfamily comprising TCRP ¥24-1*01; (xxi) TCRP ¥20 subfamily comprising e.g., one or more of TCRp ¥20-1*01, or TCRP ¥20-1*02; (xxii) TCRp ¥25 subfamily comprising TCRP ¥25-1*01; or (xxiii) TCRP ¥29 subfamily comprising TCRP ¥29-1*01; (xxiv) TCRp ¥21 subfamily; (xxv) TCRp ¥1 subfamily; (xxvi) TCRP ¥17 subfamily; (xvii) TCRP ¥23 subfamily; or (xviii) TCRP ¥26 subfamily. In some embodiments of any of the methods disclosed herein, the anti-TCRp¥ antibody molecule binds to one or more (e.g., all) of the following TCRp¥ subfamilies: (i) TCRp ¥6, e.g, TCRp ¥6-4*01, TCRp ¥6-4*02, TCRp ¥6-9*01, TCRp ¥6-8*01, TCRp ¥6-5*01, TCRp ¥6-6*02, TCRp ¥6-6*01, TCRp ¥6-2*01, TCRp ¥6-3*01 or TCRp ¥6-1*01; (ii) TCRP ¥10, e.g, TCRp ¥10-1*01, TCRp ¥10-1*02, TCRp ¥10-3*01 or TCRp ¥10-2*01; (iii) TCRp ¥12, e.g, TCRp ¥12-4*01, TCRp ¥12-3*01, or TCRp ¥12-5*01; or (iv) TCRp ¥5, e.g., TCRp ¥5-5*01, TCRp ¥5-6*01, TCRp ¥5-4*01, TCRp ¥5-8*01, TCRp ¥5-1*01. In some embodiments, the anti-TCRp¥ antibody molecule binds to TCRP ¥6, e.g., TCRp ¥6-4*01, TCRp ¥6-4*02, TCRp ¥6-9*01, TCRp ¥6-8*01, TCRp ¥6-5*01, TCRp ¥6-6*02, TCRp ¥6-6*01, TCRp ¥6-2*01, TCRp ¥6-3*01 or TCRp ¥6-1*01. In some embodiments, the anti-TCRp¥ antibody molecule binds to TCRp ¥6-5*01. In some embodiments, the anti-TCRp¥ antibody molecule does not bind to TCRp ¥12. In some embodiments, the anti-TCRP¥ antibody molecule does not bind to TCRP ¥5-5*01 or TCRp ¥5-1*01. In some embodiments of any of the methods disclosed herein, the anti-TCRp¥ antibody molecule does not bind to TCRP ¥12, or binds to TCRP ¥12 with an affinity and / or binding specificity that is less than (e.g, less than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the 16G8 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments of any of the methods disclosed herein, the anti-TCRp¥ antibody molecule binds to TCRp ¥12 with an affinity and / or binding specificity that is greater than (e.g., greater than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10-fold) the affinity and / or binding specificity of the 16G8 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments of any of the methods disclosed herein, the anti-TCRp¥ antibody molecule binds to a TCRP¥ region other than TCRP ¥12 (e.g., TCRp¥ region as described herein, e.g., TCRP ¥6 subfamily (e.g., TCRp ¥6-5*01) with an affinity and / or binding specificity that is greater than (e.g., greater than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the 16G8 murine antibody or a humanized version thereof as described in US Patent 5,861,155. 53 In some embodiments of any of the methods disclosed herein, the anti-TCRpV antibody molecule does not comprise at least one CDR of Antibody B. In some embodiments of any of the methods disclosed herein, the anti-TCRpV antibody molecule does not comprise the CDRs of Antibody B. In some embodiments of any of the methods disclosed herein, the anti-TCRpV antibody molecule does not bind to TCRP V5-5*O1 or TCRP V5-l*01, or binds to TCRP V5-5*01 or TCRP V5-l*01 with an affinity and / or binding specificity that is less than (e.g., less than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the TM23 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments of any of the methods disclosed herein, the anti-TCRpV antibody molecule binds to TCRP V5-5*01 or TCRP V5-l*01with an affinity and / or binding specificity that is greater than (e.g., greater than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the TM23 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments of any of the methods disclosed herein, the anti-TCRpV antibody molecule binds to a TCRPV region other than TCRP V5-5*01 or TCRP V5-l*01 (e.g., TCRPV region as described herein, e.g., TCRP V6 subfamily (e.g., TCRP ¥6-5*01) with an affinity and / or binding specificity that is greater than (e.g., greater than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the TM23 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments of any of the methods disclosed herein, the anti-TCRpV antibody molecule does not comprise at least one CDR of the TM23 murine antibody. In some embodiments of any of the methods disclosed herein, the anti-TCRpV antibody molecule does not comprise the CDRs of the TM23 murine antibody. In some embodiments of any of the methods disclosed herein, an anti-TCRpV antibody molecule disclosed herein does not comprise the sequence of a murine anti-rat TCR antibody R73, e.g., as disclosed in J Exp Med. 1989 Jan 1; 169(1): 73-86, herein incorporated by reference in its entirety. In some embodiments of any of the methods disclosed herein, a multispecific antibody molecule disclosed herein does not comprise the sequence of a murine anti-rat TCR antibody R73, e.g., as disclosed in J Immunol. 1993 Mar 15; 150(6):2305-15, herein incorporated by reference in its entirety. In some embodiments of any of the methods disclosed herein, an anti-TCRpV antibody molecule disclosed herein does not comprise a viral peptide-MHC complex, e.g., as disclosed in 54 Oncoimmunology. 2016; 5(1): el052930, herein incorporated by reference in its entirety. In some embodiments of any of the methods disclosed herein, a multispecific antibody molecule disclosed herein does not comprise a viral peptide-MHC complex, e.g., as disclosed in Oncoimmunology. 2016; 5(1): el052930, herein incorporated by reference in its entirety. In some embodiments of a method disclosed herein, the immune cell population comprises a T cell, a Natural Killer cell, a B cell, an antigen presenting cell, or a myeloid cell (e.g., a monocyte, a macrophage, a neutrophil or a granulocyte). In some embodiments of a method disclosed herein, the immune cell population comprises a T cell, e.g., a CD4+ T cell, a CD8+ T cell, a TCR alpha-beta T cell, or a TCR gamma-delta T cell. In some embodiments, a T cell comprises a memory T cell (e.g., a central memory T cell, or an effector memory T cell (e.g., a Temra) or an effector T cell. In some embodiments, a T cell comprises a tumor infiltrating lymphocyte (TIL). In some embodiments of a method disclosed herein, the immune cell population is obtained from a healthy subject. In some embodiments of a method disclosed herein, the immune cell population is obtained from a subject (e.g., from an apheresis sample from the subject) having a disease, e.g., a cancer, e.g., as described herein. In some embodiments, the immune cell population obtained from a subject having a disease, e.g., a cancer, comprises a tumor infiltrating lymphocyte (TIL). In some embodiments of a method disclosed herein, the method results in an expansion of at least 1.1-10 fold (e.g., at least 1.1, 1.2, 1.3, 1.4, 1.5, 2, 3, 4, 5, 6, 7, 8, 9, or 10 fold expansion). In some embodiments of a method disclosed herein, the method further comprises contacting the population of cells with an agent that promotes, e.g., increases, immune cell expansion. In some embodiments, the agent includes an immune checkpoint inhibitor, e.g., as described herein. In some embodiments, the agent includes a 4-1BB (CD127) agonist, e.g., an anti-4-lBB antibody. In some embodiments of a method disclosed herein, the method further comprises comprising contacting the population of cells with a non-dividing population of cells, e.g., feeder cells, e.g., irradiated allogenic human PBMCs. In some embodiments of a method disclosed herein, an expansion method described herein comprises expanding the cells for a period of at least about 4 hours, 6 hours, 10 hours, 12 hours, 15 hours, 18 hours, 20 hours, or 22 hours, or for at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 1,6 17, 18, 19, 20 or 21 days, or for at least about 1 week, 2 weeks, 3 weeks, 4 weeks, 5 weeks, 6 weeks, 7 weeks or 8 weeks. In some embodiments of a method disclosed herein, expansion of the population of immune cells, is compared to expansion of a similar population of cells with an antibody that binds to: a CD3 molecule, e.g., CD3 epsilon (CD3e) molecule; or a TCR alpha (TCRa) molecule. In some embodiments of a method disclosed herein, expansion of the population of immune cells, is compared to expansion of a similar population of cells not contacted with the anti-TCRpV antibody molecule. In some embodiments of a method disclosed herein, expansion of the population of memory effector T cells, e.g., Tem cells, e.g., Temra cells, is compared to expansion of a similar population of cells with an antibody that binds to: a CD3 molecule, e.g., CD3 epsilon (CD3e) molecule; or a TCR alpha (TCRa) molecule. In some embodiments of a method disclosed herein, the method results in expansion of, e.g., selective or preferential expansion of, T cells expressing a T cell receptor (TCR) comprising a TCR alpha and / or TCR beta molecule, e.g., TCR alpha-beta T cells (aP T cells). In some embodiments of a method disclosed herein, the method results in expansion of aPT cells over expansion of T cells expressing a TCR comprising a TCR gamma and / or TCR delta molecule, e.g., TCR gamma-delta T cells (76 T cells). In some embodiments, expansion of aPT cells over 76 T cells results in reduced production of cytokines associated with CRS. In some embodiments, expansion of aPT cells over 76 T cells results in immune cells that have reduced capacity to, e.g., are less prone to, induce CRS upon administration into a subject. In some embodiments of a method disclosed herein, an immune cell population (e.g., T cells (e.g., Temra cells or TILs) or NK cells) cultured in the presence of, e.g., expanded with, an anti- TCRpV antibody disclosed herein does not induce CRS and / or NT when administered into a subject, e.g., a subject having a disease or condition as described herein. In some embodiments, the anti-TCRpV antibody molecule in a multispecific molecule disclosed herein is a first immune cell engager moiety. In some embodiments, the anti-TCRpV antibody molecule does not bind to TCRP VI2, or binds to TCRP VI2 with an affinity and / or binding specificity that is less than (e.g., less than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the 16G8 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments, the anti-TCRpV antibody molecule binds to TCRP VI2 with an affinity and / or binding specificity that is greater than (e.g., greater than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the 16G8 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In 56 some embodiments, the anti-TCRpV antibody molecule binds to a TCRPV region other than TCRP V12 (e.g., TCRPV region as described herein, e.g., TCRp V6 subfamily (e.g., TCRP V6-5*01) with an affinity and / or binding specificity that is greater than (e.g., greater than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the 16G8 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments, the anti-TCRpV antibody molecule does not comprise the CDRs of the Antibody B murine antibody. In some embodiments, the anti-TCRpV antibody molecule in a multispecific molecule disclosed herein is a first immune cell engager moiety. In some embodiments, the anti-TCRpV antibody molecule does not bind to TCRP V5-5*01 or TCRp V5-1 *01, or binds to TCRP V5-5*01 or TCRP V5-l*01 with an affinity and / or binding specificity that is less than (e.g., less than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the TM23 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments, the anti-TCRpV antibody molecule binds to TCRp V5-5*01 or TCRp V5-1 *01 with an affinity and / or binding specificity that is greater than (e.g., greater than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the TM23 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments, the anti-TCRPV antibody molecule binds to a TCRpV region other than TCRP V5-5*01 or TCRp V5-1*01 (e.g., TCRPV region as described herein, e.g., TCRp V6 subfamily (e.g., TCRP V6-5*01) with an affinity and / or binding specificity that is greater than (e.g., greater than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the TM23 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments, the anti-TCRpV antibody molecule does not comprise the CDRs of the TM23 murine antibody. In some embodiments, the multispecific molecule further comprises a second immune cell engager moiety. In some embodiments, the first and / or second immune cell engager binds to and activates an immune cell, e.g., an effector cell. In some embodiments, the first and / or second immune cell engager binds to, but does not activate, an immune cell, e.g., an effector cell. In some embodiments, the second immune cell engager is chosen from an NK cell engager, a T cell engager, a B cell engager, a dendritic cell engager, or a macrophage cell engager, or a combination thereof. In some embodiments, the second immune cell engager comprises a T cell engager which binds to CD3, TCRa, TCRy, TCRL ICOS, CD28, CD27, HVEM, LIGHT, CD40, 4-1BB, 0X40, DR3, GITR, CD30, TIM1, SLAM, CD2, or CD226. In some embodiments, a multispecific molecule disclosed herein comprises a tumor targeting moiety. In some embodiment, the tumor-targeting moiety comprises an antibody molecule (e.g., Fab or scFv), a receptor molecule (e.g., a receptor, a receptor fragment or functional variant thereof), or a ligand molecule (e.g., a ligand, a ligand fragment or functional variant thereof), or a combination thereof, that binds to a cancer antigen. In some embodiments, the tumor-targeting moiety binds to a cancer antigen present on a cancer, e.g., a hematological cancer, a solid tumor, a metastatic cancer, soft tissue tumor, metastatic lesion, or a combination thereof. In some embodiments, the tumor-targeting moiety binds to a cancer antigen, e.g., BCMAorFcRH5. In some embodiments, the tumor-targeting antibody molecule binds to a conformational or a linear epitope on the tumor antigen. In some embodiments of any of the compositions or methods disclosed herein, the tumor-targeting moiety is an antigen, e.g., a cancer antigen. In some embodiments, the cancer antigen is a tumor antigen or stromal antigen, or a hematological antigen. In some embodiments of any of the compositions or methods disclosed herein, the tumor-targeting moiety binds to a cancer antigen chosen from: BCMA, FcRH5, CD19, CD20, CD22, CD30, CD33, CD38, CD47, CD99, CD123, FcRH5, CLEC12, CD179A, SLAMF7, or NY-ESO1, PDL1, CD47, gangloside 2 (GD2), prostate stem cell antigen (PSCA), prostate specific membrane antigen (PMSA), prostate-specific antigen (PSA), carcinoembryonic antigen (CEA), Ron Kinase, c-Met, Immature laminin receptor, TAG-72, BING-4, Calcium-activated chloride channel 2, Cyclin-Bl, 9D7, Ep-CAM, EphA3, Her2 / neu, Telomerase, SAP-1, Survivin, NY-ESO-l / LAGE-1, PRAME, SSX-2, Melan-A / MART-1, Gpl00 / pmell7, Tyrosinase, TRP-1 / -2, MC1R, p-catenin, BRCA1 / 2, CDK4, CML66, Fibronectin, p53, Ras, TGF-B receptor, AFP, ETA, MAGE, MUC-1, CA-125, BAGE, GAGE, NY-ESO-1, p-catenin, CDK4, CDC27, a actinin-4, TRPI / gp75, TRP2, gplOO. Melan-A / MARTl, gangliosides, WT1, EphA3, Epidermal growth factor receptor (EGFR), MART-2, MART-1, MUC1, MUC2, MUM1, MUM2, MUM3, NA88-1, NPM, OA1, OGT, RCC, RUI1, RUD, SAGE, TRG, TRP1, TSTA, Folate receptor alpha, Ll-CAM, CAIX, gpA33, GD3, GM2, VEGFR, Integrins (Integrin alphaVbeta3, Integrin alpha5Betal), Carbohydrates (Le), IGF1R, EPHA3, TRAILRI, TRAILR2, RANKL, (FAP), TGF-beta, hyaluronic acid, collagen, e.g., collagen IV, tenascin C, or tenascin W. In some embodiments of any of the compositions or methods disclosed herein, the cancer is a solid tumor including but not limited to: pancreatic (e.g., pancreatic adenocarcinoma) 58 cancer, breast cancer, colorectal cancer, lung cancer (e.g., small or non-small cell lung cancer), skin cancer, ovarian cancer, or liver cancer. In some embodiments of any of the compositions or methods disclosed herein, the cancer antigen or tumor antigen is a hematological antigen. In some embodiments, the cancer or tumor antigen is chosen from one or more of: BCMA, FcRH5, CD 19, CD20, CD22, CD30, CD33, CD38, CD47, CD99, CD123, FcRH5, CLEC12, CD179A, SLAMF7, or NY-ESO1. In some embodiments, the tumor-targeting moiety binds to one or both of BCMA or FcRH5. In some embodiments, the tumor-targeting moiety binds to BCMA. In embodiments, the tumor-targeting moiety comprises a BCMA targeting moiety. In some embodiments, the tumortargeting moiety comprising a BCMA targeting moiety binds to a BCMA antigen on the surface of a cell, e.g., a cancer or hematopoietic cell. The BCMA antigen can be present on a primary tumor cell, or a metastatic lesion thereof. In some embodiments, the cancer is a hematological cancer, e.g., multiple myeloma. For example, the BCMA antigen can be present on a tumor, e.g., a tumor of a class typified by having one or more of: limited tumor perfusion, compressed blood vessels, or fibrotic tumor interstitium. In some embodiments, the tumor targeting moiety comprising a BCMA targeting moiety comprises an anti-BCMA antibody or antigen-binding fragment thereof described in US8920776, US9243058, US9340621, US8846042, US7083785, US9545086, US7276241, US9034324, US7799902, US9387237, US8821883, US861745, US20130273055, US20160176973, US20150368351, US20150376287, US20170022284, US20160015749, US20140242077, US20170037128, US20170051068, US20160368988, US20160311915, US20160131654, US20120213768, US20110177093, US20160297885, EP3137500, EP2699259, EP2982694, EP3029068, EP3023437, WO2016090327, WO2017021450, WO2016110584, WO2016118641, WO2016168149, the entire contents of which are incorporated herein by reference. In some embodiments, the BCMA-targeting moiety includes an antibody molecule (e.g., Fab or scFv) that binds to BCMA. In some embodiments, the antibody molecule to BCMA comprises one, two, or three CDRs from any of the heavy chain variable domain sequences of Table 9, or a closely related CDR. e.g., CDRs which have at least one amino acid alteration, but not more than two, three or four alterations (e.g., substitutions, deletions, or insertions, e.g., conservative substitutions) from any of the CDR sequences of Table 9. In some embodiments, the antibody molecule to BCMA comprises a heavy chain variable domain sequence chosen from any of the amino acid sequences of Table 9, or an amino acid sequence substantially identical thereto (e.g., 95% to 99.9% identical thereto, or having at least one amino acid alteration, but not more than five, ten or fifteen alterations (e.g., substitutions, deletions, or insertions, e.g., conservative substitutions)). In some embodiments, the tumor-targeting moiety binds to FcRH5. In embodiments, the tumor-targeting moiety comprises a FcRH5 targeting moiety. In some embodiments, the tumortargeting moiety comprising a FcRH5targeting moiety binds to a FcRH5antigen on the surface of a cell, e.g., a cancer or hematopoietic cell. The FcRH5antigen can be present on a primary tumor cell, or a metastatic lesion thereof. In some embodiments, the cancer is a hematological cancer, e.g., multiple myeloma. For example, the FcRH5antigen can be present on a tumor, e.g., a tumor of a class typified by having one or more of: limited tumor perfusion, compressed blood vessels, or fibrotic tumor interstitium. In some embodiments, the tumor targeting moiety comprising a FcRH5 targeting moiety comprises an anti- FcRH5antibody or antigen-binding fragment thereof described in US Patent 7,999,077 the entire contents of which are incorporated herein by reference. In some embodiments of any of the compositions or methods disclosed herein, the cancer is a hematological cancer including, but not limited to: a B-cell or T cell malignancy, e.g., Hodgkin’s lymphoma, Non-Hodgkin’s lymphoma (e.g., B cell lymphoma, diffuse large B cell lymphoma, follicular lymphoma, chronic lymphocytic leukemia, mantle cell lymphoma, marginal zone B-cell lymphoma, Burkitt lymphoma, lymphoplasmacytic lymphoma, hairy cell leukemia), acute myeloid leukemia (AML), chronic myeloid leukemia, myelodysplastic syndrome, multiple myeloma, and acute lymphocytic leukemia. In some embodiments, the hematological cancer is multiple myeloma. In some embodiments, a multispecific molecule disclosed herein further comprises a cytokine molecule, e.g., one or two cytokine molecules. In some embodiments, the cytokine molecule is chosen from interleukin-2 (IL-2), interleukin-7 (IL-7), interleukin-12 (IL-12), interleukin-15 (IL-15), interleukin-18 (IL-18), interleukin-21 (IL-21), or interferon gamma, ora fragment, variant or combination thereof. In some embodiments, is a monomer or a dimer. In some embodiments, the cytokine molecule further comprises a receptor dimerizing domain, e.g., an IL15Ralpha dimerizing domain. In some embodiments, the cytokine molecule (e.g., IL-15) and the receptor dimerizing domain (e.g., an IL 15Ralpha dimerizing domain) are not covalently linked, e.g., are non-covalently associated. In some embodiments, a multispecific molecule disclosed herein comprises: (i) an anti-TCRpV antibody molecule (e.g., an anti-TCRpV antibody molecule as described herein); and (ii) a tumor-targeting antibody molecule (e.g., an antibody molecule that binds to a hematological antigen as described herein, e.g., chosen from one or more of BCMA, FcRH5, CD19, CD22, CD33, CD123, FcRH5, CD179a, or CLEC12). 60 In some embodiments, the multispecific molecule disclosed herein comprises the anti-TCRPV antibody molecule of (i), the tumor-targeting antibody molecule of (ii) and a cytokine molecule as described herein, e.g., an IL-12 cytokine molecule. In some embodiments, the multispecific molecule comprises an anti-TCRpV antibody molecule as described herein; and a tumor-targeting antibody molecule that binds to one or both of BCMA or FcRH5 In some embodiments, the multispecific molecule further comprises an IL-12 cytokine molecule. The multispecific molecule can be used to treat a BCMA- or FcRH5-expressing hematological cancer, e.g., multiple myeloma. In some embodiments, the multispecific molecule comprises an anti-TCRpV antibody molecule as described herein; and a tumor-targeting antibody molecule that binds one or more of CD 19, CD22, or CD 123. In some embodiments, the multispecific molecule further comprises an IL-12 cytokine molecule. The multispecific molecule can be used to treat a CD19-, CD22-, or CD 123-expressing hematological cancer, e.g., leukemia or lymphoma. In some embodiments, the CD19-, CD22-, or CD123-expressing hematological cancer is chosen from a B-cell or T cell malignancy, e.g., Hodgkin’s lymphoma, Non-Hodgkin’s lymphoma (e.g., B cell lymphoma, diffuse large B cell lymphoma, follicular lymphoma, chronic lymphocytic leukemia, mantle cell lymphoma, marginal zone B-cell lymphoma, Burkitt lymphoma, lymphoplasmacytic lymphoma, hairy cell leukemia), acute myeloid leukemia (AML), chronic myeloid leukemia, myelodysplastic syndrome, multiple myeloma, and acute lymphocytic leukemia. In some embodiments, the hematological cancer is multiple myeloma. In some embodiments, a multispecific molecule disclosed herein further comprises an immunoglobulin constant region (e.g., Fc region) chosen from the heavy chain constant regions of IgGl, IgG2, and IgG4, more particularly, the heavy chain constant region of human IgGl, IgG2 or IgG4. In some embodiments, the immunoglobulin constant region (e.g., an Fc region) is linked, e.g., covalently linked to, one or more of tumor-targeting moiety, the immune cell engager, the cytokine molecule, or the stromal modifying moiety. In some embodiments, an interface of a first and second immunoglobulin chain constant regions (e.g., Fc region) is altered, e.g., mutated, to increase or decrease dimerization, e.g., relative to a non-engineered interface. In some embodiments, the dimerization of the immunoglobulin chain constant region (e.g., Fc region) is enhanced by providing an Fc interface of a first and a second Fc region with one or more of: a paired cavity-protuberance (“knob-in-a hole”), an electrostatic interaction, or a strand-exchange, such that a greater ratio of heteromultimer:homomultimer forms, e.g., relative to a non-engineered interface. In some embodiments, In some embodiments, a multispecific molecule disclosed herein further comprises a linker, e.g., a linker described herein, optionally wherein the linker is selected from: a cleavable 61 linker, a non-cleavable linker, a peptide linker, a flexible linker, a rigid linker, a helical linker, or a non-helical linker. In some embodiments, the multispecific molecule comprises at least two non-contiguous polypeptide chains. In some embodiments, the multispecific molecule comprises the following configuration: A, B-[dimerization module]-C, -D wherein: (1) the dimerization module comprises an immunoglobulin constant domain, e.g, a heavy chain constant domain (e.g., a homodimeric or heterodimeric heavy chain constant region, e.g., an Fc region), or a constant domain of an immunoglobulin variable region (e.g., a Fab region); and (2) A, B, C, and D are independently absent; (i) an antigen binding domain that preferentially binds to a first immune cell engager comprising an anti-TCRpV antibody molecule disclosed herein; (ii) a tumor targeting moiety (e.g., a tumor-targeting antibody molecule as described herein), (iii) a second immune cell engager chosen from a T cell engager, an NK cell engager, a B cell engager, a dendritic cell engager, or a macrophage cell engager; (iv) a cytokine molecule; or (v) a stromal modifying moiety, provided that: at least one, two, or three of A, B, C, and D comprises an antigen binding domain that preferentially binds to a TCRPV region disclosed herein, and any of the remaining A, B, C, and D is absent or comprises one of a tumor targeting moiety, a second immune cell engager, a cytokine molecule, or a stromal modifying moiety. In some embodiments, the dimerization module comprises one or more immunoglobulin chain constant regions (e.g., Fc regions) comprising one or more of: a paired cavityprotuberance (“knob-in-a hole”), an electrostatic interaction, or a strand-exchange. In some embodiments, the one or more immunoglobulin chain constant regions (e.g., Fc regions) comprise an amino acid substitution at a position chosen from one or more of 347, 349, 350, 351, 366, 368, 370, 392, 394, 395, 397, 398, 399, 405, 407, or 409, e.g., of the Fc region of human IgGl. In some embodiments, the one or more immunoglobulin chain constant regions (e.g., Fc regions) comprise an amino acid substitution chosen from: T366S, L368A, or Y407V (e.g., corresponding to a cavity or hole), or T366W (e.g., corresponding to a protuberance or knob), or a combination thereof. In some embodiments, the multispecific molecule further comprises a linker, e.g., a linker between one or more of: the antigen binding domain of an anti-TCRpV antibody molecule disclosed herein and the tumor targeting moiety; the antigen binding domain of an anti-TCRpV antibody molecule disclosed herein and the second immune cell engager, the antigen binding 62 domain of an anti-TCRpV antibody molecule disclosed herein and the cytokine molecule, the antigen binding domain of an anti-TCRpV antibody molecule disclosed herein and the stromal modifying moiety, the second immune cell engager and the cytokine molecule, the second immune cell engager and the stromal modifying moiety, the cytokine molecule and the stromal modifying moiety, the antigen binding domain of an anti-TCRpV antibody molecule disclosed herein and the dimerization module, the second immune cell engager and the dimerization module, the cytokine molecule and the dimerization module, the stromal modifying moiety and the dimerization module, the tumor targeting moiety and the dimerization module, the tumor targeting moiety and the cytokine molecule, the tumor targeting moiety and the second immune cell engager, or the tumor targeting moiety and the antigen binding domain of an anti-TCRpV antibody molecule disclosed herein. In some embodiments, the linker is chosen from: a cleavable linker, a non-cleavable linker, a peptide linker, a flexible linker, a rigid linker, a helical linker, or a non-helical linker. In some embodiments, the linker is a peptide linker. In some embodiments, the peptide linker comprises Gly and Ser. In some embodiments, the peptide linker comprises an amino acid sequence chosen from SEQ ID NOs: 142-145 or 175-178. In some embodiments of a method or composition for use disclosed herein, the disease is a cancer chosen from: a hematological cancer, a solid tumor, a metastatic cancer, soft tissue tumor, metastatic lesion, or a combination thereof. In some embodiments of a method or composition for use disclosed herein, the cancer is a solid tumor chosen from: a melanoma, a pancreatic cancer (e.g., pancreatic adenocarcinoma), a breast cancer, a colorectal cancer (CRC), a lung cancer (e.g., small or non-small cell lung cancer), a skin cancer, an ovarian cancer, or a liver cancer. In some embodiments, the cancer is melanoma or CRC. In some embodiments of a method or composition for use disclosed herein the cancer is a hematological cancer chosen from: a B-cell or T cell malignancy, e.g., Hodgkin’s lymphoma, Non-Hodgkin’s lymphoma (e.g., B cell lymphoma, diffuse large B cell lymphoma, follicular lymphoma, chronic lymphocytic leukemia, mantle cell lymphoma, marginal zone B-cell lymphoma, Burkitt lymphoma, lymphoplasmacytic lymphoma, hairy cell leukemia), acute myeloid leukemia (AML), chronic myeloid leukemia, myelodysplastic syndrome, multiple myeloma, or acute lymphocytic leukemia. In some embodiments, the hematological cancer is multiple myeloma. In some embodiments, the hematological cancer is CLL or DLBCL. In some embodiments of a method or composition for use disclosed herein the sample from the subject comprises a blood sample, e.g., a peripheral blood sample, a biopsy, e.g., a tumor biopsy, or a bone marrow sample. IN some embodiments, the sample comprises a biological sample comprising immune effector cells, e.g., T cells, or NK cells. In some embodiments, T cells comprise a CD4 T cell, a CD8 T cell, (e.g., an effector T cell or a memory T cell (e.g., a memory effector T cell (e.g., Tem cell, e.g., Temra cell), or a tumor infiltrating lymphocyte (TIL). Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. Although methods and materials similar or equivalent to those described herein can be used in the practice or testing of the present invention, suitable methods and materials are described below. All publications, patent applications, patents, and other references mentioned herein are incorporated by reference in their entirety. In the case of conflict, the present specification, including definitions, will control. In addition, the materials, methods, and examples are illustrative only and are not intended to be limiting. Other features and advantages of the invention will be apparent from the following detailed description and claims. BRIEF DESCRIPTION OF THE DRAWINGS The patent or application file contains at least one drawing executed in color. Copies of this patent or patent application publication with color drawing(s) will be provided by the Office upon request and payment of the necessary fee. FIGs. 1A-1B shows the alignment of the Antibody A source mouse VH and VL framework 1, CDR 1, framework 2, CDR 2, framework 3, CDR3, and framework 4 regions with their respective humanized sequences. Kabat CDRs are shown in bold, Chothia CDRs are shown in italics, and combined CDRs are shown in boxes. The framework positions that were back mutated are double underlined. FIG. 1A shows VH sequences for murine Antibody A (SEQ ID NO: 1) and humanized Antibody A-H (SEQ ID NO: 9). FIG. IB shows VL sequences for murine Antibody A (SEQ ID NO: 2) and humanized Antibody A-H (SEQ ID NO: 10 and SEQ ID NO: 11). FIGs. 2A-2B shows the alignment of the Antibody B source mouse VH and VL framework 1, CDR 1, framework 2, CDR 2, framework 3, CDR3, and framework 4 regions with their respective humanized sequences. Kabat CDRs are shown in bold, Chothia CDRs are 64 shown in italics, and combined CDRs are shown in boxes. The framework positions that were back mutated are double underlined. FIG. 2A shows the VH sequence for murine Antibody B (SEQ ID NO: 15) and humanized VH sequences B-H. 1A to B-H. IC (SEQ IDNOs: 23-25). FIG. 2B shows the VL sequence for murine Antibody B (SEQ ID NO: 16) and humanized VL sequences B-H. ID to B-H.1H (SEQ ID NOs: 26-30). FIG. 3 depicts the phylogenetic tree of TCRBV gene family and subfamilies with corresponding antibodies mapped. Subfamily identities are as follows: Subfamily A: TCRP V6; Subfamily B: TCRp V10; Subfamily C: TCRp V12; Subfamily D: TCRp V5; Subfamily E: TCRp V7; Subfamily F: TCRp VI1; Subfamily G: TCRp V14; Subfamily H: TCRp V16; Subfamily I:TCRp V18; Subfamily J:TCRp V9; Subfamily K: TCRp V13; Subfamily L: TCRp V4; Subfamily M:TCRp V3; Subfamily N:TCRp V2; Subfamily O:TCRp V15; Subfamily P: TCRp V30; Subfamily Q: TCRp VI9; Subfamily R:TCRp V27; Subfamily S:TCRp V28; Subfamily T: TCRp V24; Subfamily U: TCRP V20; Subfamily V: TCRP V25; and Subfamily W:TCRP V29 subfamily. Subfamily members are described in detail herein in the Section titled “TCR beta V (TCRp V)”. FIGs. 4A-4C show human CD3+ T cells activated by anti-TCR Vp 13 1 antibody (A-H.l) for 6-days. Human CD3+ T cells were isolated using magnetic-bead separation (negative selection) and activated with immobilized (plate-coated) anti-TCR Vpi3.1 (A-H.l) or anti-CD3c (OKT3) antibodies at 100 nM for 6 days. FIG. 4A shows two scatter plots (left: activated with OKT3; and right: activated with A-H. 1) of expanded T cells assessed for TCR VP13.1 surface expression using anti-TCR VP13.1 (A-H.l) followed by a secondary fluorochrome- conjugated antibody for flow cytometry analysis. FIG. 4B shows percentage (%) of TCR Vpi3.1 positive T cells activated by anti-TCR Vpi3.1 (A-H.l) or anti-CD3e (OKT3) plotted against total T cells (CD3+). FIG. 4C shows relative cell count acquired by counting the number of events in each T cell subset gate (CD3 or TCR VP 13.1) for 20 seconds at a constant rate of 60pl / min. Data shown as mean value from 3 donors. FIGs. 5A-5B show cytolytic activity of human CD3+ T cells activated by anti-TCR Vp 13.1 antibody (A-H. 1) against transformed cell line RPMI 8226. FIG. 5A depicts target cell lysis of human CD3+ T cells activated with A-H.lor OKT3. Human CD3+ T cells were isolated using magnetic-bead separation (negative selection) and activated with immobilized (plate-coated) A-H. 1 or OKT3 at the indicated concentrations for 4 days prior to co-culture with RPMI 8226 cells at a (E:T) ratio of 5:1 for 2 days. Samples were next analyzed for cell lysis of RPMI 8226 cells by FACS staining for CFSE / CD138-labeled, and membrane-impermeable DNA dyes (DRAQ7) using flow cytometry analysis. FIG. 5B shows target cell lysis of human CD3+ T cells activated with A-H.l or OKT3 incubated with RPMI-8226 at a (E:T) ratio of 5:1 for 6 days 65 followed by cell lysis analysis of RPMI 8226 cells as described above. Percentage (%) target cell lysis was determined by normalizing to basal target cell lysis (i.e. without antibody treatment) using the following formula, [(x - basal) / (100% - basal), where x is cell lysis of sample]. Data shown is a representative of n=l donor. FIGs. 6A-6B show IFNg production by human PBMCs activated with the indicated antibodies. Human PBMCs were isolated from whole blood from the indicated number of donors, followed by solid-phase (plate-coated) stimulation with the indicated antibodies at lOONm. Supernatant was collected on Days 1, 2, 3, 5, or 6. FIG. 6A is a graph comparing the production of IFNg in human PBMCs activated with the antibodies indicated activated with anti-TCR Vpi3.1 antibodies (A-H.l or A-H.2) or anti-CD3e antibodies (OKT3 or SP34-2) on Day 1, 2, 3, 5, or 6 post-activation. FIG. 6B shows IFNg production in human PBMCs activated with the antibodies indicated activated with the indicated anti-TCR Vpl3.1 antibodies or anti-CD3e antibody (OKT3) on Day 1, 2, 3, 5, or 6 post-activation. FIGs. 7A-7B show IL-2 production by human PBMCs activated with the indicated antibodies. A similar experimental setup as described for FIGs 6A-6B was used. FIGs. 8A- 8B show IL-6 production by human PBMCs activated with the indicated antibodies. A similar experimental setup as described for FIGs 6A-6B was used. FIGs. 9A- 9B show TNF-alpha production by human PBMCs activated with the indicated antibodies. A similar experimental setup as described for FIGs 6A-6B was used. FIGs. 10A- 10B show IL-lbeta production by human PBMCs activated with the indicated antibodies. A similar experimental setup as described for FIGs 6A-6B was used. FIGs. 11A-1 IB are graphs showing delayed kinetics of IFNg secretion in human PMBCs activated by anti-TCR Vpi3.1 antibody A-H. 1 when compared to PBMCs activated by anti-CD3e antibody OKT3. FIG. 11A shows IFNg secretion data from 4 donors. FIG. 11B shows IFNg secretion data from 4 additional donors. Data shown is representative of n=8 donors. FIG. 12 depicts increased CD8+ TSCM and Temra T cell subsets in human PBMCs activated by anti-TCR Vp 13.1 antibodies (A-H.l or A-H.2) compared to PBMCs activated by anti-CD3e antibodies (OKT3 or SP34-2). FIGs. 13A-13F show characterization of an anti-TCRVb antibody. FIG. 13A is a graph depicting proliferation of T cells activated with anti-CD3 (OKT3) antibody or anti-TCRVb antibody. FIG. 13B shows selective expansion of CD45RA+ effector memory CD8+ and CD4+ T cells (TEMRA) cells with anti- TCRVb antibodies. Tn= naive T cell; Tscm= stem cell memory T cell; Tcm= central memory T cell; Tem=effector memory T cell; Temra=effector memory CD45RA+ T cell. FIG. 13C is a graph showing IFN-g secretion by PBMCs stimulated 66 with an anti-TCRVb antibody, or anti-CD3 antibodies. FIG. 13D shows target cell lysis by T cells stimulated with an anti-TCRVb antibody, or anti-CD3 antibodies. Cells were stimulated for 4 days followed by 2 days incubation with multiple myeloma target cells for assessment of cell killing. FIG. 13E is a graph showing perforin secretion by T cells stimulated with an anti-TCRVb antibody, or an anti-CD3 antibody. Perforin was analyzed by FACS staining in TCRVB-positive and TCRVB-negative T cells in PBMCs after 5 days of stimulation with lOOng / ml plate-bound antibody. FIG. 13F is a graph showing Granzyme B by T cells stimulated with an anti-TCRVb antibody, or an anti-CD3 antibody. Granzyme B was analyzed by FACS staining in TCRVB-positive and TCRVB-negative T cells in PBMCs after 5 days of stimulation with lOOng / ml plate-bound antibody. FIGs. 14A-14B show production of IL-2 and IL-15 and expansion of human NK cells by stimulation of PBMCs with anti-TCRVb antibody for 6 days at a dose of lOOnM. FIG. 14A shows secretion of IL-2 or IL-15 in T cells stimulated with an anti-TCRVb antibody, or anti-CD3 antibodies. FIG. 14B depicts flow cytometry dot plots showing NKp46 staining vs CD56 antibody staining in cells stimulated with an anti-TCRVb antibody or an anti-CD3 antibody or a control sample. FIGs. 15A-15C show secretion of cytokines in PBMCs stimulated with an anti-TCRVb antibody, or anti-CD3 antibodies. FIGs. 16A-16B show killing of MM cells by dual targeting BCMA-TCRvb antibody molecules. FIG. 16A shows in vitro killing by one of the following dual-targeting antibody molecules: BCMA-TCRVb (Molecule I), BCMA-CD3, or Control-TCRVb; or an isotype control. FIG. 16B shows in vivo killing of MM cells by a dual-targeting BCM-TCRVb antibody (Molecule I). FIG. 17 shows lysis of MM target cells with a dual targeting antibody (Molecule E) which recognized FcRH5 on one arm and TCRVb on the other arm. FIGs. 18A-18B demonstrate cytokine production from human PBMCs activated by anti-TCR VP8a antibodies (B-H.l) when compared to those activated by anti-CD3c antibodies (OKT3 or SP34-2). FIG. 18A shows that human PBMCs activated by anti-TCR Vp8a antibodies (B-H.l) produce similar or reduced levels of IFNy. FIG. 18B shows human PBMCs activated by anti-TCR Vp8a antibodies (B-H. 1) produce higher levels of IL-2 when compared to those activated by anti-CD3e antibodies (OKT3 or SP34-2). Data shown is representative of n = 6 donors. FIGs. 19A-19C demonstrate cytokine production from human PBMCs activated by anti-TCR Vp8a antibodies (B-H. 1). Human PBMCs activated by anti-TCR Vp8a antibodies (B-H. 1) do not significantly produce IL-6 (FIG. 19A), ILlb (FIG. 19B), and less TNFa (FIG. 19C), 67 when compared to PBMCs activated by anti-CD3c antibodies (OKT3 or SP34-2). Data shown is representative of n = 6 donors. FIGs. 20A-20E demonstrate cytokine production from human PBMCs activated by anti-TCRPV Antibody D antibody compared to control anti-CD3e antibody (OKT3). FIG. 20A shows that human PBMCs activated by anti-TCRpV Antibody D antibody produce similar or reduced levels of IFNy. FIG. 20B shows human PBMCs activated by anti-TCRpV Antibody D antibody produce higher levels of IL-2 when compared to those activated by anti-CD3c antibodies (OKT3). Human PBMCs activated by anti- TCRpV Antibody D antibody do not significantly produce IL-lbeta (FIG. 20C), IL-6, (FIG. 20D), or TNFalpha (FIG. 20E). Data shown is representative of n = 4 donors. FIGs. 21A-21B demonstrate cytokine production from human PBMCs activated by anti-TCR Vp5 antibody (Antibody E). FIG. 21A shows that human PBMCs activated by anti-TCR VP5 antibody produce similar or reduced levels of IFNy compared to PBMCS activated by anti-CD3e antibodies (OKT3 or SP34-2). FIG. 21B shows human PBMCs activated by the anti-TCR VP5 1 antibody produce higher levels of IL-2 when compared to those activated by anti-CD3c antibodies (OKT3 or SP34-2). Data shown is representative of n = 4 donors. FIGs. 22A-2D demonstrate cytokine production from human PBMCs activated by an anti-TCR VP5 antibody (Antibody E). Human PBMCs activated by anti-TCR VP5 antibody do not significantly produce IL-lbeta (FIG. 22A), IL-6, (FIG. 22B), TNFalpha (FIG. 22C), or IL-10 (FIG. 22D) as compared to PBMCs activated by anti-CD3c antibodies (OKT3 or SP34-2). Data shown is representative of n = 4 donors. FIGs. 23A-23F demonstrate cytokine production from human PBMCs activated by a dual targeting (bispecific molecule) comprising an anti-TCRpV binding moiety and a BCMA binding moiety. FIG. 23A shows that human PBMCs activated by the bispecific molecule produce similar or reduced levels of IFNy as PBMCS activated by anti-CD3e antibodies (OKT3). FIG. 23B shows human PBMCs activated by the bispecific molecule produce higher levels of IL-2 when compared to PBMCs activated by anti-CD3e antibodies (OKT3). Human PBMCs activated by the bispecific molecule do not significantly produce IL-lbeta (FIG. 23C), IL-6, (FIG. 23D), TNFalpha (FIG. 23E), or IL-10 (FIG. 23F). Data shown is representative of n = 3 donors. FIGs. 24A-24B show the structure and sequence of eight TCRPV proteins from seven different subfamilies: TCRpV6 subfamily (TCRPV6-5 and TCRPV6-4 are shown), TCRpV28 subfamily, TCRpV19 subfamily, TCRpV9 subfamily, TCRPV5 subfamily, TCRpV20 subfamily and TCRPV12 subfamily. FIG. 24A shows the structural alignment of the different TCRPV proteins. The circled area represents the outward facing region comprising the proposed binding 68 site for the anti-TCRpV antibodies disclosed herein. FIG. 24B shows the amino acid sequence alignment of the proteins shown in FIG. 24A (SEQ ID NOS 3449-3456, respectively, in order of appearance). The various TCRPV proteins (from 7 different TCRpV subfamilies) have diverse sequences but share a conserved (similar) structure and function. FIGs. 25A-25J show cytokine or chemokine secretion of PBMCs activated with anti-TCRVb antibodies (A-H.l, B-H.l), a bispecific molecule comprising an anti-TCRVb antibody (Molecule H), control isotype (122) or anti-CD3e antibody (OKT3). Data shown is representative of n = 2 donors and representative of 2 independent experiments. FIGs. 26A-26H show cytokine or chemokine secretion of PBMCs activated with anti-TCRVb antibodies (A-H.l, B-H.l), a bispecific molecule comprising an anti-TCRVb antibody (Molecule H), control isotype (122) or anti-CD3e antibody (OKT3). Data shown is representative of n = 2 donors and representative of 2 independent experiments. FIGs. 27A-27L show cytokine or chemokine secretion of PBMCs activated with anti-TCRVb antibodies (A-H.l, B-H.l), a bispecific molecule comprising an anti-TCRVb antibody (Molecule H), control isotype (122) or anti-CD3e antibody (OKT3). Data shown is representative of n = 2 donors and representative of 2 independent experiments. FIG. 28 is a graph depicting mean tumor volume in NOD / SCID / IL-2Rynull (NSG) mice engrafted with Raji-luc cells at days 10 to 28. The Star denotes PBMC implantation. Open triangles denote antibody treatment with the indicated antibodies. FIGs. 29A-B depicting Mean tumor burden (Total Flux) in NOD / SCID / IL-2Rynull (NSG) mice engrafted with cancer cells and treated with the indicated antibody. NSG mice were implanted with PBMCs on Day 1 followed by injection with cancer cells on Day 7 (Raji-luc in FIG. 29A; K562-Luc control in FIG. 29B). Antibody treatment with the indicated antibodies began on Day 16. FIG. 29A shows mean tumor burden at days 16 to 37 in NOD / SCID / IL-2Rynull (NSG) mice engrafted with Raji-luc cells. FIG. 29B shows mean tumor burden (Total Flux) at days 16 to 30 in animals engrafted with K562-luc cells. FIG. 30 is a graph depicting Mean tumor burden (Total Flux) mean tumor volume in NOD / SCID / IL-2Rynull (NSG) mice engrafted with RPMI-8226 cells. The RPMI-8226 cells were engrafted on Day 1. On Day 11, PBMCs were implanted into the mice and antibody treatment began on Day 17. FIGs. 31A-31B are graphs showing % target cell lysis at different antibody concentrations. FIG. 31A shows data generated using anti-TCR Vpi3. l / anti-CD19 (Molecule F), anti-CD3 / anti-CD19, and anti-TCR Vpl3.1 (A-H.l). FIG. 31B shows data generated using anti-TCR Vpl3 1 / anti-BCMA (Molecule G), anti-CD3 / anti-BCMA, and anti-TCR Vpi3.1 (A-H.1). FIGs. 32A-32F are graphs showing cytokine secretion stimulated by anti-TCR Vp / anti-BCMA (Molecule H) or anti-CD3 (OKT3) at Days 1, 2, 3, and 5. Cytokines examined include: IFNy, IL-2, IL-lp, IL-6, IL-10, and TNFa (FIGs. 32A-32F, respectively). FIGs. 33A-33F are graphs showing cytokine secretion stimulated by anti-TRBCl (Antibody F) or anti-CD3 (OKT3) at Days 2 and 5. Cytokines examined include: IFNy, IL-2, IL-lp, IL-6, IL-10, and TNFa (FIGs. 33A-33F, respectively). FIG. 34 is a FACS plot showing the expansion of TCRvb 6-5+ T cells over 8 days using anti-TCRvb 6-5 vl. FIG. 35 is a bar graph showing the expansion of TCRvb 6-5+ CD4+ T cells and TCRvb 6-5+ CD8+ T cells over 8 days using the anti-CD3c antibody OKT3 (lOOnM). FIG. 36 is a bar graph showing the expansion of TCRvb 6-5+ CD4+ T cells and TCRvb 6-5+ CD8+ T cells over 8 days using the anti-TCRvb 6-5 vl antibody (lOOnM). FIG. 37 is a FACS plot showing the showing the expansion of TCRvb 6-5+ T cells over 8 days using anti-TCRvb 6-5 vl or the anti-CD3c antibody OKT3. FIG. 38A is a bar graph showing the percentage of TCRPV 6-5+ T cells in PBMC cultures after 8 days of culture with the indicated antibody. Data for 5 replicates are shown. FIG. 38B is a bar graph showing the percentage of TCRPV 6-5+ T cells in purified T cell cultures after 8 days of culture with the indicated antibody. Data for 5 replicates are shown. FIG. 39A is a bar graph showing the relative count of TCRPV 6-5+ T cells in PBMC culture after 8 days of culture with the indicated antibody. FIG. 39B is a bar graph showing the relative count of TCRpV 6-5+ T cells in PBMC culture after 8 days of culture with the indicated antibody. FIG. 40A is a bar graph showing the relative count of TCRPV 6-5+ T cells in a purified T cell culture after 8 days of culture with the indicated antibody. FIG. 40B is a bar graph showing the relative count of TCRPV 6-5+ T cells in a purified T cell culture after 8 days of culture with the indicated antibody. FIG. 41 is a line graph showing the total CD3+ T cell count (fold increase) after 8 days of T cell culture with either the anti-CD3e antibody OKT3 or the anti-TCRvb 6-5 vl antibody. FIG. 42 is a series of line graphs showing the kinetics of target cells by TCRPV 6-5 vl activated T cells or anti-CD3c (OKT3) activated T cells. T cells from three different donors were utilized (donor 6769, donor 9880, donor 5411). FIG. 43A is a scatter plot showing the percent of target cell lysis by T cells by TCRPV 6-5 vl activated T cells or anti-CD3e (OKT3) activated T cells without T cell pre activation. The data is presented at day 6 of co-culture between target cells and effector T cells. FIG. 43B is a scatter plot showing the percent of target cell lysis by T cells by TCRPV 6-5 vl activated T cells 70 or anti-CD3e (OKT3) activated T cells with 4 days of T cell pre activation. The data is presented at day 2 of co-culture between target cells and effector T cells (after 4 days of T cell preactivation). FIG. 44 is a scatter plot showing the percent of target cell lysis by T cells by TCRpV 6-5 vl activated T cells or anti-CD3e (OKT3) activated T cells with 4 days of T cell pre activation. The data is presented at day 2 of co-culture between target cells and effector T cells (after 4 days of T cell pre-activation). FIG. 45 is a bar graph showing target cell lysis by T cells by TCRpV 6-5 vl activated T cells or anti-CD3e (OKT3) activated T cells (lOOnM each antibody). The data includes seven replicates of each experimental condition. FIG. 46 is a series of FACS plots that show the cell surface expression of CD3s on CD4+ TCRpV 6-5' or CD4+ TCRpV 6-5“ T cells activated with either SP34-2 (anti-CD3e antibody) or anti-TCRpV 6-5 vl (anti- TCRPV 6-5 antibody) at days 0, 1,2, 4, 6, or 8 post antibody activation. FIG. 47 is a series of FACS plots that show the cell surface expression of CD3s on CD8+ TCRpV 6-5' or CD8+ TCRpV 6-5“ T cells activated with either SP34-2 (anti-CD3s antibody) or anti-TCRpV 6-5 vl (anti- TCRPV 6-5 antibody) at days 0, 1,2, 4, 6, or 8 post antibody activation. FIG. 48 is a series of FACS plots that show the cell surface expression of TCRpV on CD4+ TCRpV 6-5' or CD4+ TCRpV 6-5+ T cells activated with either SP34-2 (anti-CD3s antibody) or anti-TCRpV 6-5 vl (anti- TCRPV 6-5 antibody) at days 0, 1,2, 4, 6, or 8 post antibody activation. FIG. 49 is a series of FACS plots that show the cell surface expression of TCRpV on CD8+ TCRpV 6-5' or CD8+ TCRpV 6-5+ T cells activated with either SP34-2 (anti-CD3s antibody) or anti-TCRpV 6-5 vl (anti- TCRpV 6-5 antibody) at days 0, 1,2, 4, 6, or 8 post antibody activation. FIG. 50A shows FACS plot of TCRpV 6-5+ cynomolgus T cell expansion either unstimulated (left) or stimulated with anti-TCRpV 6-5 vl (right) 7 days post activation of cynomolgus PBMCs. PBMCs from Donor DW8N (fresh PBMC sample, male, age 8, weight 7.9 kgs) were used. FIG. 50B shows FACS plot of TCRPV 6-5+ cynomolgus T cell expansion either unstimulated (left) or stimulated with anti-TCRpV 6-5 vl (right) 7 days post activation of cynomolgus PBMCs. PBMCs from Donor G709 (cryopreserved sample, male, age 6, weight 4.7 kgs) were used. FIG. 51 shows FACS plot and corresponding microscopy images of TCRPV 6-5+ cynomolgus T cell expansion either unstimulated (left), stimulated with SP34-2 (anti-CD3s 71 antibody) (middle); or stimulated with anti-TCRpV 6-5 vl (right) post activation of cryopreserved donor DW8N cynomolgus PBMCs. The microscopy images show the cell cluster formation (indicated by circles). FIG. 52 shows a schematic of FACS plot showing the FACS gating / staining of PBMCs prior yb T cell purification. FIG. 53 shows a schematic of FACS plot showing the FACS gating / staining of purified yb T cell population. FIG. 54 show activation of purified yb T cell population with anti-CD3c antibody (SP34-2) (left) or anti-TCRpV antibody (anti-TCRpV 6-5 vl) (right). FIG. 55A shows the release of IFNy from purified yd T cell populations activated with anti-CD3e antibody (SP34-2), anti-TCRpV antibody (anti-TCRpV 6-5 vl), or unstimulated. FIG. 55B shows the release of TNFa from purified yb T cell populations activated with anti-CD3c antibody (SP34-2), anti-TCRpV antibody (anti-TCRpV 6-5 vl), or unstimulated. FIG. 55C shows the release of IL-2 from purified yb T cell populations activated with anti-CD3s antibody (SP34-2), anti-TCRpV antibody (anti-TCRpV 6-5 vl), or unstimulated. FIG. 55D shows the release of IL-17A from purified yb T cell populations activated with anti-CD3e antibody (SP34-2), anti-TCRpV antibody (anti-TCRpV 6-5 vl), or unstimulated. FIG. 55E shows the release of IL-la from purified yb T cell populations activated with anti-CD3e antibody (SP34-2), anti-TCRpV antibody (anti-TCRpV 6-5 vl), or unstimulated. FIG. 55F shows the release of IL-ip from purified yd T cell populations activated with anti-CD3s antibody (SP34-2), anti-TCRpV antibody (anti-TCRpV 6-5 vl), or unstimulated. FIG. 55G shows the release of IL-6 from purified yb T cell populations activated with anti-CD3s antibody (SP34-2), anti-TCRpV antibody (anti-TCRpV 6-5 vl), or unstimulated. FIG. 55H shows the release of IL-10 from purified yb T cell populations activated with anti-CD3c antibody (SP34-2), anti-TCRpV antibody (anti-TCRpV 6-5 vl), or unstimulated. FIG. 56 shows the relative representations of all TCR alpha V segments (TRAV group of genes)and their variants (top), all TCR beta V segment 6-5 variants (TRBV6-5 gene) (bottom left), and all TCR beta V segments and variants excluding 6-5 (bottom right). FIG. 57A is a FACS plot showing phenotypic markers of CD4+ T cells expanded with anti-TCRpV antibody (anti-TCRpV 6-5 vl). Defined phenotypes include TEMRA (top left), Naive / TSCM (top right), TEM (bottom left), and TCM (bottom right). FIG. 57B is a FACS plot showing phenotypic markers of CD4+ T cells expanded with anti-CD3e antibody (OKT3). Defined phenotypes include TEMRA (top left), Naive / TSCM (top right), TEM (bottom left), and TCM (bottom right). FIG. 58A is a FACS plot showing phenotypic markers of CD8+ T cells expanded with 72 anti-TCRpV antibody (anti-TCRpV 6-5 vl). Defined phenotypes include TEMRA (top left), Naive / TSCM (top right), TEM (bottom left), and TCM (bottom right). FIG. 58B is a FACS plot showing phenotypic markers of CD8+ T cells expanded with anti-CD3c antibody (OKT3). Defined phenotypes include TEMRA (top left), Naive / TSCM (top right), TEM (bottom left), and TCM (bottom right). FIG. 59A is a bar graph showing the percentage of PD1 expressing CD4+ T cells from T cell cultures activated with anti-TCRpV antibody (anti-TCRpV 6-5 vl), anti-CD3s antibody (OKT3), or unstimulated. FIG. 59B is a bar graph showing the percentage of PD1 expressing CD8+ T cells from T cell cultures activated with anti-TCRpV antibody (anti-TCRpV 6-5 vl), anti-CD3s antibody (OKT3), or unstimulated. FIG. 60A is a bar graph showing the expression of Ki-67 by CD4+ T cells from T cell cultures activated with anti-TCRpV antibody (anti-TCRpV 6-5 vl), anti-CD3s antibody (OKT3), or unstimulated. FIG. 60B is a bar graph showing the expression of Ki-67 by CD8+ T cells from T cell cultures activated with anti-TCRpV antibody (anti-TCRpV 6-5 vl), anti-CD3c antibody (OKT3), or unstimulated. FIG. 61A is a FACS plot showing the percentage of TEMRA-like CD8+ T cells activated using anti-TCRpV antibody (anti-TCRpV 6-5 vl) that express CD57 (18.7%). FIG. 61B is a FACS plot showing the percentage of TEM-like CD8+ T cells activated using anti-CD3c antibody (OKT3) that express CD57 (46.8%) and the percentage of TCM-like CD8+ T cells activated using anti-CD3c antibody (OKT3) that express CD57 (18.9%). FIG. 62 shows a series of FACS plots showing the expression of expression of CD27 and by CD4+ (top) or CD8+ (bottom) T cells from T cell cultures activated with anti-TCRpV antibody (anti-TCRpV 6-5 vl), anti-CD3e antibody (OKT3), or unstimulated. FIG. 63 shows a series of FACS plots showing the expression of expression of 0X40, 4IBB, and ICOS by CD4+ (top) or CD8+ (bottom) T cells from T cell cultures activated with anti-TCRpV antibody (anti-TCRpV 6-5 vl), anti-CD3c antibody (OKT3), or unstimulated. FIG. 64 shows a series of FACS plots showing the percentage of CD3+ (CD4 gated) TCRpV 6-5+ T cells 1, 2, 3, 4, 5, 6, and 8 days port activation with BCMA and the anti-TCR Vp antibody anti-TCR VP 6-5 vl. FIG. 65A shows a series of FACS plots showing the percentage of CD4+ T cells expanded using isotype control (IgGl N297A), anti-TCRpV (anti-TCR VP 6-5 vl), or anti-CD3s (0KT3) antibodies on day 0 post activation. FIG. 65B shows a series of FACS plots showing the percentage of CD4+ T cells expanded using isotype control (IgGl N297A), anti-TCRPV (anti-TCR VP 6-5 vl), or anti-CD3e (OKT3) antibodies on day 1 post activation. FIG. 65C shows a series of FACS plots showing the percentage of CD4+ T cells expanded using 73 isotype control (IgG 1 N297A), anti-TCRpV (anti-TCR Vp 6-5 v I), or anti-CD3e (OKT3) antibodies on day 2 post activation. FIG. 65D shows a series of FACS plots showing the percentage of CD4+ T cells expanded using isotype control (IgGl N297A), anti-TCRpV (anti-TCR VP 6-5 vl), or anti-CD3s (OKT3) antibodies on day 3 post activation. FIG. 65E shows a series of FACS plots showing the percentage of CD4+ T cells expanded using isotype control (IgGl N297A), anti-TCRpV (anti-TCR Vp 6-5 vl), or anti-CD3s (OKT3) antibodies on day 4 post activation. FIG. 65F shows a series of FACS plots showing the percentage of CD4+ T cells expanded using isotype control (IgGl N297A), anti-TCRpV (anti-TCR Vp 6-5 vl), or anti-CD3s (OKT3) antibodies on day 5 post activation. FIG. 65G shows a series of FACS plots showing the percentage of CD4+ T cells expanded using isotype control (IgGl N297A), anti-TCRpV (anti-TCR Vp 6-5 vl), or anti-CD3e (OKT3) antibodies on day 6 post activation. FIG. 65H shows a series of FACS plots showing the percentage of CD4+ T cells expanded using isotype control (IgGl N297A), anti-TCRpV (anti-TCR VP 6-5 vl), or anti-CD3s (OKT3) antibodies on day 8 post activation. FIG. 66A is a bar graph showing ATP production from glycolysis of T cell cultures activated with the indicated antibodies. FIG. 66B is a bar graph showing ATP production from oxidative phosphorylation of T cell cultures activated with the indicated antibodies. FIG. 67 is a line graph showing the oxygen consumption rate (OCR) of T cells from about 0 to 75 minutes activated with the indicated antibody. FIG. 68A shows the oxygen consumption rate (OCR) of T cells activated with the indicated antibody during basal respiration. FIG. 68B shows the oxygen consumption rate (OCR) of T cells activated with the indicated antibody during maximal respiration. FIG. 68C shows the oxygen consumption rate (OCR) of T cells activated with the indicated antibody during spare respiratory capacity. FIG. 68D is a line graph indicates the areas of basal respiration and maximal respiration as shown in FIG. 68A and FIG. 68B, respectively. FIG. 69A is a bar graph showing ATP production from glycolysis of T cell cultures activated with anti-TCRpV 6-5 vl and re-stimulated with the indicated antibody. FIG. 69B is a bar graph showing ATP production from oxidative phosphorylation of T cell cultures activated with anti-TCRpV 6-5 vl and re-stimulated with the indicated antibody. FIGS. 70A-70G are graphs showing expression of IFNg, TNFa, IL-la, IL-lb, IL-6 (CRS and neurotoxicity associated cytokines) with BHM1710 (anti TCRVB), a reduced affinity anti CD3 antibody (TB) and the SP34 anti CD3e antibody. FIG. 71 is a FACS plot showing the percentage of NK cells expanded from T cell cultures activated with the indicated antibody. FIG. 72 is a bar graph showing the number of NK cells expanded from T cell cultures 74 activated with the indicated antibody. FIG. 73 shows a series of FACS plots showing NK cell proliferation induced by T cell cultures activated with the indicated antibody. FIG. 74 is a schematic showing an assay described in Example for determining NK cell mediated lysis of target K562 cells. FIG. 75 is a bar graph showing the percent target cell lysis mediated by NK cells activated by PBMCs activated with the indicated antibody. FIG. 76 shows a series of FACS plots showing the proliferation of NK cells from PBMC cultures activated / expanded with the indicated antibody (isotype control or OKT3). PBMCs from three donors (DI, D2, and D3) were analyzed. FIG. 77 shows a series of FACS plots showing the proliferation of NK cells from PBMC cultures activated / expanded with the indicated antibody (anti-TCRvP 12-3 / 4 vl or anti-TCRvP 12-3 / 4 v2). PBMCs from three donors (DI, D2, and D3) were analyzed. FIG. 78 shows a series of FACS plots showing the proliferation of NK cells from PBMC cultures activated / expanded with the indicated antibody (anti-TCRvP 12-3 / 4 v3 or SP34-2). PBMCs from three donors (DI, D2, and D3) were analyzed. FIG. 79 is a bar graph showing the level of secreted IFNy by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, OKT3, or SP34) and cultured with said antibody for the indicated number of days (1, 3, or 5). FIG. 80 is a bar graph showing the level of secreted IL-2 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, OKT3, or SP34) and cultured with said antibody for the indicated number of days (1, 3, or 5). FIG. 81 is a bar graph showing the level of secreted IL-15 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, OKT3, or SP34) and cultured with said antibody for the indicated number of days (1, 3, or 5). FIG. 82 is a bar graph showing the level of secreted IL-ip by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, OKT3, or SP34) and cultured with said antibody for the indicated number of days (1, 3, or 5). FIG. 83 is a bar graph showing the level of secreted IL-6 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, OKT3, or SP34) and cultured with said antibody for the indicated number of days (1, 3, or 5). FIG. 84 is a bar graph showing the level of secreted IL-10 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, OKT3, or SP34) and cultured with said antibody for the indicated number of days (1, 3, or 5). FIG. 85 is a bar graph showing the level of the indicated cytokine secreted by T cells 75 activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl or SP34). The data includes use of 17 individual PBMC donors. FIG. 86A is a bar graph showing the level of secreted IFNy by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl or OKT3) and cultured with said antibody for the indicated number of days (1, 2, 3, 5, or 6). FIG. 86B is a bar graph showing the level of secreted IL-1 p by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl or OKT3) and cultured with said antibody for the indicated number of days (1, 2, 3, 5, or 6). FIG. 86C is a bar graph showing the level of secreted IL-4 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl or OKT3) and cultured with said antibody for the indicated number of days (1, 2, 3, 5, or 6). FIG. 86D is a bar graph showing the level of secreted IL-6 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl or OKT3) and cultured with said antibody for the indicated number of days (1, 2, 3, 5, or 6). FIG. 86E is a bar graph showing the level of secreted IL-10 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl or OKT3) and cultured with said antibody for the indicated number of days (1, 2, 3, 5, or 6). FIG. 86F is a bar graph showing the level of secreted TNFa by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl or OKT3) and cultured with said antibody for the indicated number of days (1, 2, 3, 5, or 6). FIG. 86G is a bar graph showing the level of secreted IL-2 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl or OKT3) and cultured with said antibody for the indicated number of days (1, 2, 3, 5, or 6). FIG. 87A is a bar graph showing the level of secreted IFNy by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, anti-TCRpV 6-5 vl, OKT3, SP34-2, or isotype control) and cultured with said antibody for the indicated number of days (1, 2, 3, 5, or 6). FIG. 87B is a bar graph showing the level of secreted IL-ip by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, anti-TCRpV 6-5 vl, OKT3, SP34-2, or isotype control) and cultured with said antibody for the indicated number of days (1, 2, 3, 5, or 6). FIG. 87C is a bar graph showing the level of secreted IL-4 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, anti-TCRpV 6-5 vl, OKT3, SP34-2, or isotype control) and cultured with said antibody for the indicated number of days (1, 2, 3, 5, or 6). FIG. 87D is a bar graph showing the level of secreted IL-6 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, anti-TCRpV 6-5 vl, OKT3, SP34-2, or isotype control) and cultured with said antibody for the indicated number of days (1, 2, 3, 5, or 6). FIG. 87E is a bar graph showing the level of secreted IL-10 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, anti-TCRpV 6-5 vl, OKT3, SP34-2, or isotype control) and cultured with said antibody for the indicated number of 76 days (1, 2, 3, 5, or 6). FIG. 87F is a bar graph showing the level of secreted TNFa by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, anti-TCRpV 6-5 vl, OKT3, SP34-2, or isotype control) and cultured with said antibody for the indicated number of days (1, 2, 3, 5, or 6). FIG. 87G is a bar graph showing the level of secreted IL-2 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, anti-TCRpV 6-5 vl, OKT3, SP34-2, or isotype control) and cultured with said antibody for the indicated number of days (1, 2, 3, 5, or 6). FIG. 88A is a bar graph showing the level of secreted IFNy by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, anti-TCRpV 6-5 vl, OKT3, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 88B is a bar graph showing the level of secreted IL-1 p by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, anti-TCRpV 6-5 vl, OKT3, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 88C is a bar graph showing the level of secreted IL-4 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, anti-TCRpV 6-5 vl, OKT3, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 88D is a bar graph showing the level of secreted IL-6 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, anti-TCRpV 6-5 vl, OKT3, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 88E is a bar graph showing the level of secreted IL-10 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, anti-TCRpV 6-5 vl, OKT3, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 88F is a bar graph showing the level of secreted TNFa by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, anti-TCRpV 6-5 vl, OKT3, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 88G is a bar graph showing the level of secreted IL-2 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, anti-TCRpV 6-5 vl, OKT3, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 89A is a bar graph showing the level of secreted IL-17A by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, OKT3, or SP34-2) and cultured with said antibody for the indicated number of days (2, 5, or 7). FIG. 89B is a bar graph showing the level of secreted IL-17A by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, OKT3, or SP34-2) and cultured with said antibody for the indicated number of days (2, 5, or 8). FIG. 89C is a bar graph showing the level of secreted IL-17A by T 77 cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl, OKT3, or SP34-2) and cultured with said antibody for the indicated number of days (2, 5, or 7). FIG. 89D is a bar graph showing the level of secreted IL-17A by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl or SP34-2) and cultured with said antibody for the indicated number of days (1, 3, 5, or 7). FIG. 90A is a bar graph showing the level of secreted IFNy by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRpV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90B is a bar graph showing the level of secreted IL-ip by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRpV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90C is a bar graph showing the level of secreted IL-4 by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRpV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90D is a bar graph showing the level of secreted IL-6 by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRPV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90E is a bar graph showing the level of secreted IL-10 by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRpV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90F is a bar graph showing the level of secreted TNFa by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRPV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90G is a bar graph showing the level of secreted IL-2 by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRpV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90H is a bar graph showing the level of secreted IL-12p70 by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRpV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 901 is a bar graph showing the level of secreted IL-13 by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-78 BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRpV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90J is a bar graph showing the level of secreted IL-8 by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRPV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90K is a bar graph showing the level of secreted exotaxin by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRpV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90L is a bar graph showing the level of secreted exotoxin-3 by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRpV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90M is a bar graph showing the level of secreted IL-8 by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRpV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90N is a bar graph showing the level of secreted IP-10 by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRPV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 900 is a bar graph showing the level of secreted MCP-1 by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRpV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90P is a bar graph showing the level of secreted MCP-4 by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRPV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1,2,3,4, 5, 6, or 8). FIG. 90Qis a bar graph showing the level of secreted MDC by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRpV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90R is a bar graph showing the level of secreted MIP-la by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRPV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90S is a bar graph showing the level of secreted MIP-lb by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-79 BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRpV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90T is a bar graph showing the level of secreted TARC by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRPV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 901 is a bar graph showing the level of secreted GMCSF by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRpV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90V is a bar graph showing the level of secreted IL-12-23p40 by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRpV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90W is a bar graph showing the level of secreted IL-15 by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRpV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90X is a bar graph showing the level of secreted IL-16 by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRPV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90Y is a bar graph showing the level of secreted IL-17a by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRpV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90Z is a bar graph showing the level of secreted IL-la by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRPV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90AA is a bar graph showing the level of secreted IL-5 by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRpV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90BB is a bar graph showing the level of secreted IL-7 by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRPV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90CC is a bar graph showing the level of secreted TNF-B by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-80 BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRpV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1, 2, 3, 4, 5, 6, or 8). FIG. 90DD is a bar graph showing the level of secreted VEGF by T cells activated / expanded with the indicated antibody (isotype control; anti-TCRpV 6-5 vl with anti-BCMA antibody; anti-TCRpV 6-5 vl; anti-TCRPV 123 / 4 vl, or SP34-2) and cultured with said antibody for the indicated number of days (1,2,3,4, 5, 6, or 8). FIG. 91 shows a graphical representation of the relation of sequences between different TCRVB clonotype subfamilies. FIG. 92A is a bar graph showing the percentage of cytokine release from PBMCs activated / expanded for eight days using the indicated antibody (anti-TCRpV 12-3 / 4 vl or SP34-2). FIG. 92B is a bar graph showing the percentage of cytokine release from PBMCs activated / expanded for eight days using the indicated antibody (anti-TCRpV 5 or SP34-2). FIG. 92C is a bar graph showing the percentage of cytokine release from PBMCs activated / expanded for eight days using the indicated antibody (anti-TCRpV 10 or SP34-2). FIG. 93A a bar graph showing the level of secreted IFNy by T cells activated / expanded with the indicated antibody for the indicated number of days (3 or 6). FIG. 93B a bar graph showing the level of secreted IL-10 by T cells activated / expanded with the indicated antibody for the indicated number of days (3 or 6). FIG. 93C a bar graph showing the level of secreted IL-17A by T cells activated / expanded with the indicated antibody for the indicated number of days (3 or 6). FIG. 93D a bar graph showing the level of secreted IL-la by T cells activated / expanded with the indicated antibody for the indicated number of days (3 or 6). FIG. 93E a bar graph showing the level of secreted IL-1 p by T cells activated / expanded with the indicated antibody for the indicated number of days (3 or 6). FIG. 93F a bar graph showing the level of secreted IL-6 by T cells activated / expanded with the indicated antibody for the indicated number of days (3 or 6). FIG. 93G a bar graph showing the level of secreted TNFa by T cells activated / expanded with the indicated antibody for the indicated number of days (3 or 6). FIG. 93H a bar graph showing the level of secreted IL-2 by T cells activated / expanded with the indicated antibody for the indicated number of days (3 or 6). FIG. 94 is a bar graph summarizing data from FACS analysis of PBMCs activated / expanded for 6 days using the indicated anti-TCRVP antibody. FIG. 95A a bar graph showing the level of secreted IFNy by T cells activated / expanded with the indicated antibody for the indicated number of days (1, 3, 5, or 7). FIG. 95B a bar graph showing the level of secreted IL-10 by T cells activated / expanded with the indicated antibody for the indicated number of days (1, 3, 5, or 7). FIG. 95C a bar graph showing the level of secreted IL-17A by T cells activated / expanded with the indicated antibody for the 81 indicated number of days (1, 3, 5, or 7). FIG. 95D a bar graph showing the level of secreted IL-la by T cells activated / expanded with the indicated antibody for the indicated number of days (1, 3, 5, or 7). FIG. 95E a bar graph showing the level of secreted IL-ip by T cells activated / expanded with the indicated antibody for the indicated number of days (1, 3, 5, or 7). FIG. 95F a bar graph showing the level of secreted IL-6 by T cells activated / expanded with the indicated antibody for the indicated number of days (1, 3, 5, or 7). FIG. 95G a bar graph showing the level of secreted IL-4 by T cells activated / expanded with the indicated antibody for the indicated number of days (1, 3, 5, or 7). FIG. 95H a bar graph showing the level of secreted IL-2 by T cells activated / expanded with the indicated antibody for the indicated number of days (1, 3, 5, or 7). FIG. 96 is a bar graph summarizing data from FACS analysis of PBMCs activated / expanded for 7 days using the indicated anti-TCRVP antibody. FIG. 97A is a bar graph showing the level of secreted IFNy by T cells activated / expanded with the indicated antibody for the indicated number of days (3 or 6). FIG. 97B a bar graph showing the level of secreted IL-10 by T cells activated / expanded with the indicated antibody for the indicated number of days (3 or 6). FIG. 97C a bar graph showing the level of secreted IL-17A by T cells activated / expanded with the indicated antibody for the indicated number of days (3 or 6). FIG. 97D a bar graph showing the level of secreted IL-la by T cells activated / expanded with the indicated antibody for the indicated number of days (3 or 6). FIG. 97E a bar graph showing the level of secreted IL-ip by T cells activated / expanded with the indicated antibody for the indicated number of days (3 or 6). FIG. 97F a bar graph showing the level of secreted IL-6 by T cells activated / expanded with the indicated antibody for the indicated number of days (3 or 6). FIG. 97G a bar graph showing the level of secreted IL-4 by T cells activated / expanded with the indicated antibody for the indicated number of days (3 or 6). FIG. 97H a bar graph showing the level of secreted TNFa by T cells activated / expanded with the indicated antibody for the indicated number of days (3 or 6). FIG. 971 a bar graph showing the level of secreted IL-2 by T cells activated / expanded with the indicated antibody for the indicated number of days (3 or 6). FIG. 98A is a bar graph showing the level of secreted IFN-y by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl (plate coated), anti-CD3c (plate coated), anti-TCRpV 6-5 vl (in solution), or anti-CD3s (in solution) and cultured with said antibody for the indicated number of days (1, 3, 5, or 7). FIG. 98B is a bar graph showing the level of secreted IFN-y by T cells activated / expanded with the indicated antibody (anti-TCRPV 6-5 vl (plate coated), anti-CD3e (plate coated), anti-TCRpV 6-5 vl (in solution), or anti-CD3c (in solution) and cultured with said antibody for the indicated number of days (1, 3, 5, 82 or 7). FIG. 98C is a bar graph showing the level of secreted IL-lb by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl (plate coated), anti-CD3s (plate coated), anti-TCRPV 6-5 vl (in solution), or anti-CD3s (in solution) and cultured with said antibody for the indicated number of days (1, 3, 5, or 7). FIG. 98D is a bar graph showing the level of secreted IL-6 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl (plate coated), anti-CD3s (plate coated), anti-TCRpV 6-5 vl (in solution), or anti-CD3e (in solution) and cultured with said antibody for the indicated number of days (1, 3, 5, or 7). FIG. 98E is a bar graph showing the level of secreted IL-10 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl (plate coated), anti-CD3s (plate coated), anti-TCRpV 6-5 vl (in solution), or anti-CD3s (in solution) and cultured with said antibody for the indicated number of days (1, 3, 5, or 7). FIG. 98F is a bar graph showing the level of secreted IL-15 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl (plate coated), anti-CD3s (plate coated), anti-TCRpV 6-5 vl (in solution), or anti-CD3a (in solution) and cultured with said antibody for the indicated number of days (1, 3, 5, or 7). FIG. 98G is a bar graph showing the level of secreted IL-17A by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl (plate coated), anti-CD3s (plate coated), anti-TCRpV 6-5 vl (in solution), or anti-CD3e (in solution) and cultured with said antibody for the indicated number of days (1, 3, 5, or 7) FIG. 98H is a bar graph showing the level of secreted IL-la by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl (plate coated), anti-CD3s (plate coated), anti-TCRPV 6-5 vl (in solution), or anti-CD3e (in solution) and cultured with said antibody for the indicated number of days (1, 3, 5, or 7). FIG. 981 is a bar graph showing the level of secreted IL-lb by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl (plate coated), anti-CD3s (plate coated), anti-TCRpV 6-5 vl (in solution), or anti-CD3e (in solution) and cultured with said antibody for the indicated number of days (1, 3, 5, or 7). FIG. 98J is a bar graph showing the level of secreted IL-2 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl (plate coated), anti-CD3s (plate coated), anti-TCRpV 6-5 vl (in solution), or anti-CD3s (in solution) and cultured with said antibody for the indicated number of days (1, 3, 5, or 7). FIG. 98K is a bar graph showing the level of secreted IL-4 by T cells activated / expanded with the indicated antibody (anti-TCRpV 6-5 vl (plate coated), anti-CD3c (plate coated), anti-TCRpV 6-5 vl (in solution), or anti-CD3s (in solution) and cultured with said antibody for the indicated number of days (1, 3, 5, or 7). FIG. 98L is a bar graph showing the level of secreted TNF-a by T cells activated / expanded with the indicated antibody (anti-TCRPV 6-5 vl (plate coated), anti-CD3e (plate coated), anti-TCRpV 6-5 vl (in solution), or anti-CD3s (in solution) and cultured with said antibody for the indicated number of days (1, 3, 5, or 7). FIG. 99 is a FACS plot showing the showing the ability of MH3-2 to bind PBMCs from one of two donors when the PBMCs are either preincubated with TM23 or not (MH3-2 Alone). FIG. 100 is a FACS plot showing the ability of MH3-2 to bind PBMCs from one of two donors when the PBMCs are either preincubated with TM23 or not (MH3-2 Alone). FIG. 101A is a bar graph showing the polyfunctional strength index (PSI) of PBMC CD4+ T cells, CD4+ T cells expanded with anti-CD3 antibody, (CD3 Expanded T cells), and CD4+ T cells expanded with anti-TCRVp 6-5 antibody (Drug Expanded T cells). The Effector mediators are Granzyme B, IFNy, MIP-la, perforin, TNFa, and TNFp. The Stimulatory mediators are IL-5. The Chemoattractive mediators are MIP-lb. FIG. 101B is a bar graph showing the polyfunctional strength index (PSI) of PBMC CD8+ T cells, CD8+ T cells expanded with anti-CD3 antibody, (CD3 Expanded T cells), and CD8+ T cells expanded with anti-TCRVp 6-5 antibody (Drug Expanded T cells). The Effector mediators are Granzyme B, IFNy, MIP-la, perforin, and TNFp. The Chemoattractive mediators are MIP-lb and RANTES. FIGs. 102A-102C show binding of a CD19xTCRvP bispecific molecule to a TCR molecule. FIG. 102A is a schematic of the bispecific molecule used in this study. FIG. 102B is a graph showing the binding of a CD19xTCRvP bispecific molecule to soluble TCR. FIG. 102C is a graph showing binding of a CD19xTCRvP bispecific molecule to TCR expressed on Jurkat cells. FIGs. 103A-103D show the characterization of a murine CD19xTCRvP 13-2 / 3 (2x2) bispecific molecule. FIG. 103A is a schematic of the bispecific molecule used in this study. FIG. 103B is a graph showing the binding kinetics of murine CD19xTCRvP 13-2 / 3. FIG. 103C are dot plots showing the expansion of TCRVB+ T cells following a 6 day incubation with murine CD19xTCRvp 13-2 / 3. FIG. 103D is a graph showing the relative count of splenic B cells after a 6 day in vitro incubation with murine CD19xTCRvp 13-2 / 3 bispecific antibody. FIG. 104 are graphs showing the level of B cells in the blood or spleen of animals treated with 0.1 mg per kg or 1 mg per kg of a murine CD19xTCRvP 13-2 / 3 bispecific antibody. FIGs. 105A-105B are graphs showing the level of NK cells (FIG. 105A) or T cells (FIG. 105B) in the blood or spleen of animals treated with 0.1 mg per kg or 1 mg per kg of a murine CD19xTCRvP 13-2 / 3 bispecific antibody. FIGs. 106A-106F show expansion of TCRVB+ T cells and lysis of target cells with a CD19xTCRvp bispecific molecule. FIG. 106A is a schematic of the bi specific molecule used in this study. FIG. 106B is a graph showing target cell lysis by pre-expanded TCRVB+ T cells or CD3+ expanded pan T cells. FIG. 106C shows depletion of purified B cells by purified T cells treated with a CD19xTCRvP bispecific molecule. FIG. 106D shows depletion of purified B cells by purified T cells treated with a CD19xCD3 bispecific molecule. FIG. 106E shows depletion 84 of B cells in a PBMC preparation treated with a CD19xTCRvP bispecific molecule. FIG. 106F shows depletion of B cells in a PBMC preparation treated with a CD19xCD3 bispecific molecule. FIGs. 107A-107B are graphs showing the expression of various cytokines from PBMCs treated with a CD19 x CD3 bispecific molecule (FIG. 107A) or a CD19xTCRVB 6-5 bispecific molecule (FIG. 107B). FIGs. 108A-108C show a CD 19 x TCRvP 6-5 (2x2) pharmacokinetic (PK) profile and dosing strategy. FIG. 108A is a schematic of the experimental design. FIG. 108B is a graph showing the concentration of CD 19 x TCRvP 6-5 at the indicated timepoints after treatment. FIG. 108C shows the detection reagents used to detect CD19 x TCRvp 6-5. DETAILED DESCRIPTION OF THE INVENTION Current bispecific constructs designed to redirect T cells to promote tumor cell lysis for cancer immunotherapy typically utilize antibody fragments (Fab, scFv, VH, etc.) that are derived from monoclonal antibodies (mAb) directed against the CD3e subunit of the T cell receptor (TCR). However, there are limitations to this approach which may prevent the full realization of the therapeutic potential for such bispecific constructs. Previous studies have shown that even low “activating” doses of anti-CD3e mAb can cause long-term T cell dysfunction and exert immunosuppressive effects. In addition, anti-CD3e mAbs have been associated with side effects that result from massive T cell activation. The large number of activated T cells secrete substantial amounts of cytokines, the most important of which is Interferon gamma (IFNg). This excess amount of IFNg in turn activates macrophages which then overproduce proinflammatory cytokines such as IL-lbeta, IL-6, IL-10 and TNF-alpha, causing a “cytokine storm” known as the cytokine release syndrome (CRS) (Shimabukuro-Vornhagen et al., J Immunother Cancer. 2018 Jun 15;6(1):56, herein incorporated by reference in its entirety). Thus, the need exists for developing antibodies that are capable of binding and activating only a subset of effector T cells, e.g., to reduce the CRS and / or neurotoxicity (NT). This invention features molecules targeting the TCRpV chain of TCR and methods thereof. Without wishing to be bound by theory, such molecules are capable of binding, activating, and / or expanding only a subset of T cells, avoiding or reducing CRS and / or NT and minimizing potential immunosuppressive effects of anti-CD3 mAbs. TCR is a di sulfide-linked membrane-anchored heterodimeric protein normally consisting of the highly variable alpha (a) and beta (p) chains expressed as part of a complex with the invariant CD3 chain molecules. TCR on ap T cells is formed by a heterodimer of one alpha 85 chain and one beta chain. Each alpha or beta chain consists of a constant domain and a highly variable domain classified as the Immunoglobulin superfamily (IgSF) fold. The TCRPV chains can be further classified into 30 subfamilies (TRBV1-30). Despite their high structural and functional homology, the amino acid sequence homology in the TRBV genes is very low. Only 4 amino acids out of ~95 are identical while 10 additional amino acids are conserved among all subfamilies (see an alignment of TCRBV amino acid sequences in Table 9). Nevertheless, TCRs formed between alpha and beta chains of highly diverse sequences show a remarkable structural homology (FIGs. 24A and 24B) and elicit a similar function, e.g., activation of T cells. Disclosed herein is the discovery of a novel class of antibodies, i.e., anti-TCRpV antibody molecules disclosed herein, which despite having low sequence similarity (e.g., low sequence identity among the different antibody molecules that recognize different TCRPV subfamilies), recognize a structurally conserved, yet sequence-wise variable, region, e.g., domain, on the TCRpV protein (as denoted by the circled area in FIG. 24A) and have a similar function (e.g., activation of T cells and a similar cytokine profile as described herein). Thus, the anti-TCRpV antibody molecules disclosed herein share a structure-function relationship. Without wishing to be bound by theory, it is believed that in some embodiments, the anti-TCRpV antibody molecules disclosed herein bind to an outward facing epitope of a TCRpV protein when it is in a complex with a TCRalpha protein, e.g., as denoted by the circled area in FIG. 24A. In some embodiments, the anti-TCRpV antibody molecules disclosed herein recognize (e.g., bind to), a domain (e.g., an epitope) on the TCRpV protein that is: (1) structurally conserved among different TCRpV subfamilies; and (2) has minimal sequence identity among the different TCRPV subfamilies. As shown in Table 9, TCRPV proteins from the different TCRBV subfamilies share minimal sequence similarity. However, as shown in FIG. 24A-B, TCRpV proteins which have minimal sequence similarity, share a similar 3D conformation and structure. In some embodiments, the anti-TCRpV antibody molecules disclosed herein do not recognize, e.g., bind to, an interface of a TCRpV:TCRalpha complex. In some embodiments, the anti-TCRpV antibody molecules disclosed herein do not recognize, e.g., bind to, a constant region of a TCRPV protein. In some embodiments, the anti-TCRpV antibody molecules disclosed herein do not recognize, e.g., bind to, one or more (e.g., all) of a complementarity determining region (e.g., CDR1, CDR2 and / or CDR3) of a TCRpV protein. This disclosure provides, inter alia, antibody molecules directed to the variable chain of the beta subunit of TCR (TCRPV) which bind and, e.g., activate a subset of T cells. The anti-TCRPV antibody molecules disclosed herein result in lesser or no production of cytokines associated with CRS, e.g., IL-6, IL-lbeta, IL-10 and TNF alpha; and enhanced and / or delayed production of IL-2 and IFNg. In some embodiments, the anti-TCRpV antibodies disclosed herein have a cytokine profile, e.g., as described herein, which differs from a cytokine profile of a T cell engager that binds to a receptor or molecule other than a TCRPV region (“a non-TCRpV-binding T cell engager”). In some embodiments, the anti-TCRpV antibodies disclosed herein result in expansion of TCRPV+ T cells, e.g., a subset of memory effector T cells known as Temra. Without wishing to be bound by theory, it is believed that in some embodiments, Temra cells can promote tumor cell lysis but not CRS. Accordingly, provided herein are methods of making said anti-TCRpV antibody molecules and uses thereof. Also disclosed herein are multispecific molecules, e.g., bispecific molecules comprising said anti-TCRpV antibody molecules. In some embodiments, compositions comprising anti-TCRpV antibody molecules of the present disclosure, can be used, e.g., to: (1) activate and redirect T cells to promote tumor cell lysis for cancer immunotherapy; and / or (2) expand TCRpV+ T cells. In some embodiments, compositions comprising anti-TCRpV antibody molecules as disclosed herein limit the harmful side-effects of CRS and / or NT, e.g., CRS and / or NT associated with anti-CD3e targeting. In some embodiments, the anti-TCRpV antibody molecule does not bind to TCRp VI2, or binds to TCRp V12 with an affinity and / or binding specificity that is less than (e.g., less than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the 16G8 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments, the anti-TCRpV antibody molecule binds to TCRP V12 with an affinity and / or binding specificity that is greater than (e.g., greater than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the 16G8 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments, the anti-TCRpV antibody molecule binds to a TCRPV region other than TCRP ¥12 (e.g., TCRPV region as described herein, e.g., TCRP V6 subfamily (e.g., TCRP V6-5*01) with an affinity and / or binding specificity that is greater than (e.g., greater than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the 16G8 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments, the anti-TCRPV antibody molecule does not comprise the CDRs of the Antibody B murine antibody. In some embodiments, the anti-TCRpV antibody molecule does not bind to TCRP V5-5*01 or TCRp V5-l*01, or binds to TCRp V5-5*01 or TCRp V5-l*01 with an affinity and / or binding specificity that is less than (e.g., less than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the TM23 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments, the anti-TCRpV antibody molecule binds to TCRP V5-5*01 or TCRP V5-l*01with an affinity and / or binding specificity that is greater than (e.g., greater than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the TM23 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments, the anti-TCRpV antibody molecule binds to a TCRPV region other than TCRp V5-5*01 or TCRP V5-l*01 (e.g., TCRPV region as described herein, e.g., TCRP V6 subfamily (e.g., TCRP V6-5*01) with an affinity and / or binding specificity that is greater than (e.g., greater than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the TM23 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments, the anti-TCRpV antibody molecule does not comprise the CDRs of the TM23 murine antibody. Accordingly, provided herein are, inter alia, anti-TCRpV antibody molecules, multispecific or multifunctional molecules (e.g., multispecific or multifunctional antibody molecules) that comprise anti-TCRpV antibody molecules, nucleic acids encoding the same, methods of producing the aforesaid molecules, pharmaceutical compositions comprising aforesaid molecules, and methods of treating a disease or disorder, e.g., cancer, using the aforesaid molecules. The antibody molecules and pharmaceutical compositions disclosed herein can be used (alone or in combination with other agents or therapeutic modalities) to treat, prevent and / or diagnose disorders and conditions, e.g., cancer, e.g., as described herein. Definitions Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which the invention pertains. The term “a” and “an” refers to one or to more than one (i.e., to at least one) of the grammatical object of the article. By way of example, “an element” means one element or more than one element. The term “about” when referring to a measurable value such as an amount, a temporal duration, and the like, is meant to encompass variations of ±20% or in some instances ±10%, or in some instances ±5%, or in some instances ±1%, or in some instances ±0.1% from the specified value, as such variations are appropriate to perform the disclosed methods. The term “acquire” or “acquiring” as the terms are used herein, refer to obtaining possession of a physical entity (e.g., a sample, a polypeptide, a nucleic acid, or a sequence), or a value, e.g., a numerical value, by “directly acquiring” or “indirectly acquiring” the physical entity or value. “Directly acquiring” means performing a process (e.g., performing a synthetic or analytical method) to obtain the physical entity or value. “Indirectly acquiring” refers to receiving the physical entity or value from another party or source (e.g., a third party laboratory that directly acquired the physical entity or value). Directly acquiring a physical entity includes performing a process that includes a physical change in a physical substance, e.g., a starting material. Directly acquiring a value includes performing a process that includes a physical change in a sample or another substance, e.g., performing an analytical process which includes a physical change in a substance, e.g., a sample. As used herein, the term “T cell receptor beta variable chain” or “TCRPV,” refers to an extracellular region of the T cell receptor beta chain which comprises the antigen recognition domain of the T cell receptor. The term TCRPV includes isoforms, mammalian, e.g., human TCRPV, species homologs of human and analogs comprising at least one common epitope with TCRPV. Human TCRPV comprises a gene family comprising subfamilies including, but not limited to: a TCRp ¥6 subfamily, a TCRp V10 subfamily, a TCRP ¥12 subfamily, a TCRP V5 subfamily, a TCRp ¥7 subfamily, a TCRP ¥11 subfamily, a TCRP ¥14 subfamily, a TCRp ¥16 subfamily, a TCRp ¥18 subfamily, a TCRp ¥9 subfamily, a TCRp ¥13 subfamily, a TCRp ¥4 subfamily, a TCRp ¥3 subfamily, a TCRP ¥2 subfamily, a TCRp ¥15 subfamily, a TCRp ¥30 subfamily, a TCRp ¥19 subfamily, a TCRp ¥27 subfamily, a TCRp ¥28 subfamily, a TCRp ¥24 subfamily, a TCRP ¥20 subfamily, TCRP ¥25 subfamily, a TCRP ¥29 subfamily, a TCRP ¥1 subfamily, a TCRP ¥17 subfamily, a TCRP ¥21 subfamily, a TCRP ¥23 subfamily, or a TCRP ¥26 subfamily, as well as family members of said subfamilies, and variants thereof (e.g., a structural or functional variant thereof). In some embodiments, the TCRp ¥6 subfamily comprises: TCRp ¥6-4*01, TCRp ¥6-4*02, TCRp ¥6-9*01, TCRp ¥6-8*01, TCRp ¥6-5*01, TCRp ¥6-6*02, TCRp ¥6-6*01, TCRp ¥6-2*01, TCRp ¥6-3*01 or TCRp ¥6-1*01. In some embodiments, TCRPV comprises TCRp V6-5*01, or a variant thereof, e.g., a variant having 85%, 90%, 95%, 99% or more identity the naturally-occurring sequence. TCRP V6-5*01 is also known as TRBV65; TCRBV6S5; TCRBV13S1, or TCRp V13.1. The amino acid sequence of TCRP V6-5*01, e.g., human TCRP V6-5*01, is known in that art, e.g., as provided by IMGT ID L36092. In some embodiments, TCRp V6-5*01 is encoded by the nucleic acid sequence of SEQ ID NO: 43, or a sequence having 85%, 90%, 95%, 99% or more identity thereof. In some embodiments, TCRP V6-5*01 comprises the amino acid sequence of SEQ ID NO: 44, or a sequence having 85%, 90%, 95%, 99% or more identity thereof. The term “human-like antibody molecule” as used herein refers to a humanized antibody molecule, human antibody molecule or an antibody molecule having at least 95% identity with a non-murine germline framework region, e.g., FR1, FR2, FR3 and / or FR4. In some embodiments, the human-like antibody molecule comprises a framework region having at least 95% identity to a human germline framework region, e.g., a FR1, FR2, FR3 and / or FR4 of a human germline framework region. In some embodiments, the human-like antibody molecule is a recombinant antibody. In some embodiments, the human-like antibody molecule is a humanized antibody molecule. In some embodiments, the human-like antibody molecule is human antibody molecule. In some embodiments, the human-like antibody molecule is a phage display or a yeast display antibody molecule. In some embodiments, the human-like antibody molecule is a chimeric antibody molecule. In some embodiments, the human-like antibody molecule is a CDR grafted antibody molecule. The term “cytokine profile” as used herein, refers to the level and / or activity of on one or more cytokines or chemokines, e.g., as described herein. In some embodiments, a cytokine profile comprises the level and / or activity of a naturally occurring cytokine, a fragment or a variant thereof. In an embodiment, a cytokine profile comprises the level and / or activity of one or more cytokines and / or one or more chemokines (e.g., as described herein). In some embodiments, a cytokine profile comprises the level and / or activity of a naturally occurring cytokine, a fragment or a variant thereof. In some embodiments, a cytokine profile comprises the level and / or activity of a naturally occurring chemokine, a fragment or a variant thereof. In an embodiment, a cytokine profile comprises the level and / or activity of one or more of: IL-2 (e.g., full length, a variant, or a fragment thereof); IL-lbeta (e.g., full length, a variant, or a fragment thereof); IL-6 (e.g., full length, a variant, or a fragment thereof); TNFa (e.g., full length, a variant, or a fragment thereof); IFNg (e.g., full length, a variant, or a fragment thereof) IL-10 (e.g., full length, a variant, or a fragment thereof); IL-4 (e.g., full length, a variant, or a fragment thereof); TNF alpha (e.g., full length, a variant, or a fragment thereof);IL-12p70 (e.g., full length, a variant, or a fragment thereof); IL-13 (e.g., full length, a variant, or a fragment thereof); IL-8 (e.g., full length, a variant, or a fragment thereof); Eotaxin (e.g., full length, a variant, or a fragment thereof); Eotaxin-3 (e.g., full length, a variant, or a fragment thereof); IL-8 (HA) (e.g., full length, a variant, or a fragment thereof); IP-10 (e.g., full length, a variant, or a fragment thereof); MCP-1 (e.g., full length, a variant, or a fragment thereof); MCP-4 (e.g., full length, a variant, or a fragment thereof); MDC (e.g., full length, a variant, or a fragment thereof); MIP-la (e.g., full length, a variant, or a fragment thereof); MIP-lb (e.g., full length, a variant, or a fragment thereof); TARC (e.g., full length, a variant, or a fragment thereof); GM-CSF (e.g., full length, a variant, or a fragment thereof); IL-12 23p40 (e.g., full length, a variant, or a fragment thereof); IL-15 (e.g., full length, a variant, or a fragment thereof); IL-16 (e.g., full length, a variant, or a fragment thereof); IL-17a (e.g., full length, a variant, or a fragment thereof); IL-la (e.g., full length, a variant, or a fragment thereof); IL-5 (e.g., full length, a variant, or a fragment thereof); IL-7 (e.g., full length, a variant, or a fragment thereof); TNF-beta (e.g., full length, a variant, or a fragment thereof); or VEGF (e.g., full length, a variant, or a fragment thereof). In some embodiments, a cytokine profile includes secretion of one or more cytokines or chemokines. In an embodiment, a cytokine in a cytokine profile can be modulated, e.g., increased or decreased, by an anti-TCRBV antibody molecule described herein. In one embodiment, the cytokine profile includes cytokines associated with a cytokine storm or cytokine release syndrome (CRS), e.g., IL-6, IL-lbeta, TNFalpha and IL-10. The term “variant” refers to a polypeptide that has a substantially identical amino acid sequence to the naturally-occurring sequence, or are encoded by a substantially identical nucleotide sequence. In some embodiments, the variant is a functional variant. In some embodiments, a TCRpV variant can bind to TCRa and form a TCR a:p complex. The term “functional variant” refers to a polypeptide that has a substantially identical amino acid sequence to the naturally-occurring sequence, or are encoded by a substantially identical nucleotide sequence, and are capable of having one or more activities of the naturally-occurring sequence. As used herein, a “multifunctional” or a “multispecific” molecule refers to molecule, e.g., a polypeptide, that has two or more functionalities, e.g., two or more binding specificities. In some embodiments, the functionalities can include one or more immune cell engagers, one or more tumor binding molecules, one or more cytokine molecules, one or more stromal modifiers, and other moieties described herein. In some embodiments, the multispecific molecule is a multispecific antibody molecule, e.g., a bispecific antibody molecule. In some embodiments, the multispecific molecule includes an anti-TCRVb antibody molecule as described herein. In some embodiments, the multifunctional molecule includes an immune cell engager. “An immune cell engager” refers to one or more binding specificities that bind and / or activate an immune cell, e.g., a cell involved in an immune response. In embodiments, the immune cell is chosen from a T cell, an NK cell, a B cell, a dendritic cell, and / or the macrophage cell. The immune cell engager can be an antibody molecule, a receptor molecule (e.g., a full length receptor, receptor fragment, or fusion thereof (e.g., a receptor-Fc fusion)), or a ligand molecule (e.g., a full length ligand, ligand fragment, or fusion thereof (e.g., a ligand-Fc fusion)) that binds to the immune cell antigen (e.g., the T cell, the NK cell antigen, the B cell antigen, the dendritic cell antigen, and / or the macrophage cell antigen). In embodiments, the immune cell engager specifically binds to the target immune cell, e.g., binds preferentially to the target immune cell. For example, when the immune cell engager is an antibody molecule, it binds to an immune cell antigen (e.g., a T cell antigen, an NK cell antigen, a B cell antigen, a dendritic cell antigen, and / or a macrophage cell antigen) with a dissociation constant of less than about 10 nM. In some embodiments, the multifunctional molecule includes a cytokine molecule. As used herein, a “cytokine molecule” refers to full length, a fragment or a variant of a cytokine; a cytokine further comprising a receptor domain, e.g., a cytokine receptor dimerizing domain; or an agonist of a cytokine receptor, e.g., an antibody molecule (e.g., an agonistic antibody) to a cytokine receptor, that elicits at least one activity of a naturally-occurring cytokine. In some embodiments the cytokine molecule is chosen from interleukin-2 (IL-2), interleukin-7 (IL-7), interleukin-12 (IL-12), interleukin-10 (IL-10), interleukin-15 (IL-15), interleukin-18 (IL-18), interleukin-21 (IL-21), or interferon gamma, or a fragment or variant thereof, or a combination of any of the aforesaid cytokines. The cytokine molecule can be a monomer or a dimer. In embodiments, the cytokine molecule can further include a cytokine receptor dimerizing domain. In other embodiments, the cytokine molecule is an agonist of a cytokine receptor, e.g., an antibody molecule (e.g., an agonistic antibody) to a cytokine receptor chosen from an IL-15Ra or IL-21R. As used herein, the term “molecule” as used in, e.g., antibody molecule, cytokine molecule, receptor molecule, includes full-length, naturally-occurring molecules, as well as variants, e.g., functional variants (e.g., truncations, fragments, mutated (e.g., substantially similar sequences) or derivatized form thereof), so long as at least one function and / or activity of the unmodified (e.g., naturally-occurring) molecule remains. In some embodiments, the multifunctional molecule includes a stromal modifying moiety. A “stromal modifying moiety,” as used herein refers to an agent, e.g., a protein (e.g., an enzyme), that is capable of altering, e.g., degrading a component of, the stroma. In embodiments, the component of the stroma is chosen from, e.g., an ECM component, e.g., a 92 glycosaminoglycan, e.g., hyaluronan (also known as hyaluronic acid or HA), chondroitin sulfate, chondroitin, dermatan sulfate, heparin sulfate, heparin, entactin, tenascin, aggrecan and keratin sulfate; or an extracellular protein, e.g., collagen, laminin, elastin, fibrinogen, fibronectin, and vitronectin. Certain terms are defined below. As used herein, the articles “a” and “an” refer to one or more than one, e.g., to at least one, of the grammatical object of the article. The use of the words "a" or "an" when used in conjunction with the term "comprising" herein may mean "one," but it is also consistent with the meaning of "one or more," "at least one," and "one or more than one." As used herein, “about” and “approximately” generally mean an acceptable degree of error for the quantity measured given the nature or precision of the measurements. Exemplary degrees of error are within 20 percent (%), typically, within 10%, and more typically, within 5% of a given range of values. “Antibody molecule” as used herein refers to a protein, e.g., an immunoglobulin chain or fragment thereof, comprising at least one immunoglobulin variable domain structure and / or sequence. An antibody molecule encompasses antibodies (e.g., full-length antibodies) and antibody fragments. In an embodiment, an antibody molecule comprises an antigen binding or functional fragment of a full length antibody, or a full length immunoglobulin chain. For example, a full-length antibody is an immunoglobulin (Ig) molecule (e.g., an IgG antibody) that is naturally occurring or formed by normal immunoglobulin gene fragment recombinatorial processes). In embodiments, an antibody molecule refers to an immunologically active, antigenbinding portion of an immunoglobulin molecule, such as an antibody fragment. An antibody fragment, e.g., functional fragment, is a portion of an antibody, e.g., Fab, Fab', F(ab')2, F(ab)2, variable fragment (Fv), domain antibody (dAb), or single chain variable fragment (scFv). A functional antibody fragment binds to the same antigen as that recognized by the intact (e.g., full-length) antibody. The terms “antibody fragment” or “functional fragment” also include isolated fragments consisting of the variable regions, such as the “Fv” fragments consisting of the variable regions of the heavy and light chains or recombinant single chain polypeptide molecules in which light and heavy variable regions are connected by a peptide linker (“scFv proteins”). In some embodiments, an antibody fragment does not include portions of antibodies without antigen binding activity, such as Fc fragments or single amino acid residues. Exemplary antibody molecules include full length antibodies and antibody fragments, e.g., dAb (domain antibody), single chain, Fab, Fab’, and F(ab’)2 fragments, and single chain variable fragments (scFvs). In some embodiments, the antibody molecule is an antibody mimetic. In some embodiments, the antibody molecule is, or comprises, an antibody-like framework or scaffold, such as, fibronectins, ankyrin repeats (e.g., designed ankyrin repeat proteins (DARPins)), avimers, affibody affinity ligands, anticalins, or affilin molecules. As used herein, an “immunoglobulin variable domain sequence” refers to an amino acid sequence which can form the structure of an immunoglobulin variable domain. For example, the sequence may include all or part of the amino acid sequence of a naturally-occurring variable domain. For example, the sequence may or may not include one, two, or more N- or C-terminal amino acids, or may include other alterations that are compatible with formation of the protein structure. In embodiments, an antibody molecule is monospecific, e.g., it comprises binding specificity for a single epitope. In some embodiments, an antibody molecule is multispecific, e.g., it comprises a plurality of immunoglobulin variable domain sequences, where a first immunoglobulin variable domain sequence has binding specificity for a first epitope and a second immunoglobulin variable domain sequence has binding specificity for a second epitope. In some embodiments, an antibody molecule is a bispecific antibody molecule. “Bispecific antibody molecule” as used herein refers to an antibody molecule that has specificity for more than one (e.g., two, three, four, or more) epitope and / or antigen. “Antigen” (Ag) as used herein refers to a molecule that can provoke an immune response, e.g., involving activation of certain immune cells and / or antibody generation. Any macromolecule, including almost all proteins or peptides, can be an antigen. Antigens can also be derived from genomic recombinant or DNA. For example, any DNA comprising a nucleotide sequence or a partial nucleotide sequence that encodes a protein capable of eliciting an immune response encodes an “antigen.” In embodiments, an antigen does not need to be encoded solely by a full length nucleotide sequence of a gene, nor does an antigen need to be encoded by a gene at all. In embodiments, an antigen can be synthesized or can be derived from a biological sample, e.g., a tissue sample, a tumor sample, a cell, or a fluid with other biological components. As used, herein a “tumor antigen” or interchangeably, a “cancer antigen” includes any molecule present on, or associated with, a cancer, e.g., a cancer cell or a tumor microenvironment that can provoke an immune response. As used, herein an “immune cell antigen” includes any molecule present on, or associated with, an immune cell that can provoke an immune response. The “antigen-binding site,” or “binding portion” of an antibody molecule refers to the part of an antibody molecule, e.g., an immunoglobulin (Ig) molecule, that participates in antigen binding. In embodiments, the antigen binding site is formed by amino acid residues of the variable (V) regions of the heavy (H) and light (L) chains. Three highly divergent stretches 94 within the variable regions of the heavy and light chains, referred to as hypervariable regions, are disposed between more conserved flanking stretches called “framework regions,” (FRs). FRs are amino acid sequences that are naturally found between, and adjacent to, hypervariable regions in immunoglobulins. In embodiments, in an antibody molecule, the three hypervariable regions of a light chain and the three hypervariable regions of a heavy chain are disposed relative to each other in three dimensional space to form an antigen-binding surface, which is complementary to the three-dimensional surface of a bound antigen. The three hypervariable regions of each of the heavy and light chains are referred to as “complementarity-determining regions,” or “CDRs.” The framework region and CDRs have been defined and described, e.g., in Kabat, E.A., et al. (1991) Sequences of Proteins of Immunological Interest, Fifth Edition, U.S. Department of Health and Human Services, NIH Publication No. 91-3242, and Chothia, C et al. (1987) J. Mol. Biol. 196:901-917. Each variable chain (e.g., variable heavy chain and variable light chain) is typically made up of three CDRs and four FRs, arranged from amino-terminus to carboxy-terminus in the amino acid order: FR1, CDR1, FR2, CDR2, FR3, CDR3, and FR4. “Cancer” as used herein can encompass all types of oncogenic processes and / or cancerous growths. In embodiments, cancer includes primary tumors as well as metastatic tissues or malignantly transformed cells, tissues, or organs. In embodiments, cancer encompasses all histopathologies and stages, e.g., stages of invasiveness / severity, of a cancer. In embodiments, cancer includes relapsed and / or resistant cancer. The terms “cancer” and “tumor” can be used interchangeably. For example, both terms encompass solid and liquid tumors. As used herein, the term “cancer” or “tumor” includes premalignant, as well as malignant cancers and tumors. As used herein, an “immune cell” refers to any of various cells that function in the immune system, e.g., to protect against agents of infection and foreign matter. In embodiments, this term includes leukocytes, e.g., neutrophils, eosinophils, basophils, lymphocytes, and monocytes. Innate leukocytes include phagocytes (e.g., macrophages, neutrophils, and dendritic cells), mast cells, eosinophils, basophils, and natural killer cells. Innate leukocytes identify and eliminate pathogens, either by attacking larger pathogens through contact or by engulfing and then killing microorganisms, and are mediators in the activation of an adaptive immune response. The cells of the adaptive immune system are special types of leukocytes, called lymphocytes. B cells and T cells are important types of lymphocytes and are derived from hematopoietic stem cells in the bone marrow. B cells are involved in the humoral immune response, whereas T cells are involved in cell-mediated immune response. The term “immune cell” includes immune effector cells. “Immune effector cell,” as that term is used herein, refers to a cell that is involved in an immune response, e.g., in the promotion of an immune effector response. Examples of immune effector cells include, but are not limited to, T cells, e.g., alpha / beta T cells and gamma / delta T cells, B cells, natural killer (NK) cells, natural killer T (NK T) cells, and mast cells. The term “effector function” or “effector response” refers to a specialized function of a cell. Effector function of a T cell, for example, may be cytolytic activity or helper activity including the secretion of cytokines. The compositions and methods of the present invention encompass polypeptides and nucleic acids having the sequences specified, or sequences substantially identical or similar thereto, e.g., sequences at least 80%, 85%, 90%, 95% identical or higher to the sequence specified. In the context of an amino acid sequence, the term "substantially identical" is used herein to refer to a first amino acid that contains a sufficient or minimum number of amino acid residues that are i) identical to, or ii) conservative substitutions of aligned amino acid residues in a second amino acid sequence such that the first and second amino acid sequences can have a common structural domain and / or common functional activity. For example, amino acid sequences that contain a common structural domain having at least about 80%, 85%, 90%. 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identity to a reference sequence, e.g., a sequence provided herein. In the context of nucleotide sequence, the term "substantially identical" is used herein to refer to a first nucleic acid sequence that contains a sufficient or minimum number of nucleotides that are identical to aligned nucleotides in a second nucleic acid sequence such that the first and second nucleotide sequences encode a polypeptide having common functional activity, or encode a common structural polypeptide domain or a common functional polypeptide activity. For example, nucleotide sequences having at least about 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identity to a reference sequence, e.g., a sequence provided herein. The term “variant” refers to a polypeptide that has a substantially identical amino acid sequence to a reference amino acid sequence, or is encoded by a substantially identical nucleotide sequence. In some embodiments, the variant is a functional variant. The term “functional variant” refers to a polypeptide that has a substantially identical amino acid sequence to a reference amino acid sequence, or is encoded by a substantially identical nucleotide sequence, and is capable of having one or more activities of the reference amino acid sequence. Calculations of homology or sequence identity between sequences (the terms are used interchangeably herein) are performed as follows. 96 To determine the percent identity of two amino acid sequences, or of two nucleic acid sequences, the sequences are aligned for optimal comparison purposes (e.g., gaps can be introduced in one or both of a first and a second amino acid or nucleic acid sequence for optimal alignment and non-homologous sequences can be disregarded for comparison purposes). In a preferred embodiment, the length of a reference sequence aligned for comparison purposes is at least 30%, preferably at least 40%, more preferably at least 50%, 60%, and even more preferably at least 70%, 80%, 90%, 100% of the length of the reference sequence. The amino acid residues or nucleotides at corresponding amino acid positions or nucleotide positions are then compared. When a position in the first sequence is occupied by the same amino acid residue or nucleotide as the corresponding position in the second sequence, then the molecules are identical at that position (as used herein amino acid or nucleic acid "identity" is equivalent to amino acid or nucleic acid "homology"). The percent identity between the two sequences is a function of the number of identical positions shared by the sequences, taking into account the number of gaps, and the length of each gap, which need to be introduced for optimal alignment of the two sequences. The comparison of sequences and determination of percent identity between two sequences can be accomplished using a mathematical algorithm. In a preferred embodiment, the percent identity between two amino acid sequences is determined using the Needleman and Wunsch ((1970) J. Mol. Biol. 48:444-453 ) algorithm which has been incorporated into the GAP program in the GCG software package (available at http: / / www.gcg.com), using either a Blossum 62 matrix or a PAM250 matrix, and a gap weight of 16, 14, 12, 10, 8, 6, or 4 and a length weight of 1, 2, 3, 4, 5, or 6. In yet another preferred embodiment, the percent identity between two nucleotide sequences is determined using the GAP program in the GCG software package (available at http: / / www.gcg.com), using aNWSgapdna.CMP matrix and a gap weight of 40, 50, 60, 70, or 80 and a length weight of 1, 2, 3, 4, 5, or 6. A particularly preferred set of parameters (and the one that should be used unless otherwise specified) are a Blossum 62 scoring matrix with a gap penalty of 12, a gap extend penalty of 4, and a frameshift gap penalty of 5. The percent identity between two amino acid or nucleotide sequences can be determined using the algorithm of E. Meyers and W. Miller ((1989) CABIOS, 4:11-17) which has been incorporated into the ALIGN program (version 2.0), using a PAM120 weight residue table, a gap length penalty of 12 and a gap penalty of 4. The nucleic acid and protein sequences described herein can be used as a "query sequence" to perform a search against public databases to, for example, identify other family members or related sequences. Such searches can be performed using the NBLAST and 97 XBLAST programs (version 2.0) of Altschul, et al. (1990) J. Mol. Biol. 215:403-10. BLAST nucleotide searches can be performed with the NBLAST program, score = 100, wordlength = 12 to obtain nucleotide sequences homologous to a nucleic acid molecule of the invention. BLAST protein searches can be performed with the XBLAST program, score = 50, wordlength = 3 to obtain amino acid sequences homologous to protein molecules of the invention. To obtain gapped alignments for comparison purposes, Gapped BLAST can be utilized as described in Altschul et al., (1997) Nucleic Acids Res. 25:3389-3402. When utilizing BLAST and Gapped BLAST programs, the default parameters of the respective programs {e.g., XBLAST and NBLAST) can be used. It is understood that the molecules of the present invention may have additional conservative or non-essential amino acid substitutions, which do not have a substantial effect on their functions. The term "amino acid" is intended to embrace all molecules, whether natural or synthetic, which include both an amino functionality and an acid functionality and capable of being included in a polymer of naturally-occurring amino acids. Exemplary amino acids include naturally-occurring amino acids; analogs, derivatives and congeners thereof; amino acid analogs having variant side chains; and all stereoisomers of any of any of the foregoing. As used herein the term "amino acid" includes both the D- or L- optical isomers and peptidomimetics. A "conservative amino acid substitution" is one in which the amino acid residue is replaced with an amino acid residue having a similar side chain. Families of amino acid residues having similar side chains have been defined in the art. These families include amino acids with basic side chains {e.g., lysine, arginine, histidine), acidic side chains {e.g., aspartic acid, glutamic acid), uncharged polar side chains {e.g., glycine, asparagine, glutamine, serine, threonine, tyrosine, cysteine), nonpolar side chains {e.g., alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan), beta-branched side chains {e.g., threonine, valine, isoleucine) and aromatic side chains {e.g., tyrosine, phenylalanine, tryptophan, histidine). The terms "polypeptide", "peptide" and "protein" (if single chain) are used interchangeably herein to refer to polymers of amino acids of any length. The polymer may be linear or branched, it may comprise modified amino acids, and it may be interrupted by nonamino acids. The terms also encompass an amino acid polymer that has been modified; for example, disulfide bond formation, glycosylation, lipidation, acetylation, phosphorylation, or any other manipulation, such as conjugation with a labeling component. The polypeptide can be isolated from natural sources, can be a produced by recombinant techniques from a eukaryotic or prokaryotic host, or can be a product of synthetic procedures. The terms "nucleic acid," "nucleic acid sequence," "nucleotide sequence," or "polynucleotide sequence," and "polynucleotide" are used interchangeably. They refer to a polymeric form of nucleotides of any length, either deoxyribonucleotides or ribonucleotides, or analogs thereof. The polynucleotide may be either single-stranded or double-stranded, and if single-stranded may be the coding strand or non-coding (antisense) strand. A polynucleotide may comprise modified nucleotides, such as methylated nucleotides and nucleotide analogs. The sequence of nucleotides may be interrupted by non-nucleotide components. A polynucleotide may be further modified after polymerization, such as by conjugation with a labeling component. The nucleic acid may be a recombinant polynucleotide, or a polynucleotide of genomic, cDNA, semisynthetic, or synthetic origin which either does not occur in nature or is linked to another polynucleotide in a non-natural arrangement. The term "isolated," as used herein, refers to material that is removed from its original or native environment (e.g., the natural environment if it is naturally occurring). For example, a naturally-occurring polynucleotide or polypeptide present in a living animal is not isolated, but the same polynucleotide or polypeptide, separated by human intervention from some or all of the co-existing materials in the natural system, is isolated. Such polynucleotides could be part of a vector and / or such polynucleotides or polypeptides could be part of a composition, and still be isolated in that such vector or composition is not part of the environment in which it is found in nature. Various aspects of the invention are described in further detail below. Additional definitions are set out throughout the specification. Human T cell receptor (TCR) complex T cell receptors (TCR) can be found on the surface of T cells. TCRs recognize antigens, e.g., peptides, presented on, e.g., bound to, major histocompatibility complex (MHC) molecules on the surface of cells, e.g., antigen-presenting cells. TCRs are heterodimeric molecules and can comprise an alpha chain, a beta chain, a gamma chain or a delta chain. TCRs comprising an alpha chain and a beta chain are also referred to as TCRap. The TCR beta chain consists of the following regions (also known as segments): variable (V), diversity (D), joining (J) and constant (C) (see Mayer G. and Nyland J. (2010) Chapter 10: Major Histocompatibility Complex and T-cell Receptors-Role in Immune Responses. In: Microbiology and Immunology on-line, University of South Carolina School of Medicine). The TCR alpha chain consists of V, J and C regions. The rearrangement of the T-cell receptor (TCR) through somatic recombination of V (variable), D (diversity), J (joining), and C (constant) regions is a defining event in the development and maturation of a T cell. TCR gene rearrangement takes place in the thymus. TCRs can comprise a receptor complex, known as the TCR complex, which comprises a TCR heterodimer comprising of an alpha chain and a beta chain, and dimeric signaling molecules, e.g., CD3 co-receptors, e.g., CD38 / s, and / or CD3y / s. TCR beta V (TCRpV) Diversity in the immune system enables protection against a huge array of pathogens. Since the germline genome is limited in size, diversity is achieved not only by the process of V(D)J recombination but also by junctional (junctions between V-D and D-J segments) deletion of nucleotides and addition of pseudo-random, non-templated nucleotides. The TCR beta gene undergoes gene arrangement to generate diversity. The TCR V beta repertoire varies between individuals and populations because of, e.g., 7 frequently occurring inactivating polymorphisms in functional gene segments and a large insertion / deletion-related polymorphism encompassing 2 V beta gene segments. This disclosure provides, inter alia, antibody molecules and fragments thereof, that bind, e.g., specifically bind, to a human TCR beta V chain (TCRPV), e.g., a TCRpV gene family (also referred to as a group), e.g., a TCRpV subfamily (also referred to as a subgroup), e.g., as described herein. TCR beta V families and subfamilies are known in the art, e.g., as described in Yassai et al., (2009) Immunogenetics 61(7)pp:493-502; Wei S. and Concannon P. (1994) Human Immunology 41(3) pp: 201-206. The antibodies described herein can be recombinant antibodies, e.g., recombinant non-murine antibodies, e.g., recombinant human or humanized antibodies. The terms TCRBV, TCRVB, TRBV, TCRPV, TCRVP or TRPV are used interchangeably herein and refer to a TCR beta V chain, e.g., as described herein. In an aspect, the disclosure provides an anti-TCRpV antibody molecule that binds to human TCRPV, e.g., a TCRPV family, e.g., gene family or a variant thereof. In some embodiments a TCRBV gene family comprises one or more subfamilies, e.g., as described herein, e.g., in FIG. 3, Table 8A or Table 8B. In some embodiments, the TCRPV gene family comprises: a TCRP V6 subfamily, a TCRp V10 subfamily, a TCRp V12 subfamily, a TCRp V5 subfamily, a TCRP V7 subfamily, a TCRp VI1 subfamily, a TCRp V14 subfamily, a TCRP V16 subfamily, a TCRp VI8 subfamily, a TCRp V9 subfamily, a TCRP VI3 subfamily, a TCRP V4 subfamily, a TCRP V3 subfamily, a TCRp V2 subfamily, a TCRP VI5 subfamily, a TCRp V30 subfamily, a TCRP V19 subfamily, a TCRP V27 subfamily, a TCRP V28 subfamily, a TCRp V24 subfamily, a TCRp V20 subfamily, TCRP V25 subfamily, a TCRP V29 subfamily, a TCRp VI subfamily, a TCRP VI7 subfamily, a TCRp V21 subfamily, a TCRp V23 subfamily, or a TCRP V26 subfamily. In some embodiments, TCRp V6 subfamily is also known as TCRp VI3.1. In some embodiments, the TCRP V6 subfamily comprises: TCRP V6-4*01, TCRP V6-4*02, TCRP V6-9*01, TCRp V6-8*01, TCRp V6-5*01, TCRp V6-6*02, TCRp V6-6*01, TCRp V6-2*01, TCRp V6-3*01 or TCRP V6-l*01, or a variant thereof. In some embodiments, TCRP V6 comprises TCRP V6-4*01, or a variant thereof. In some embodiments, TCRP V6 comprises TCRP V6-4*02, or a variant thereof. In some embodiments, TCRP V6 comprises TCRp V6-9*01, or a variant thereof. In some embodiments, TCRP V6 comprises TCRP V6-8*01, or a variant thereof. In some embodiments, TCRp V6 comprises TCRp V6-5*01, or a variant thereof. In some embodiments, TCRP V6 comprises TCRP V6-6*02, or a variant thereof. In some embodiments, TCRp V6 comprises TCRp V6-6*01, or a variant thereof. In some embodiments, TCRp V6 comprises TCRp V6-2*01, or a variant thereof. In some embodiments, TCRP V6 comprises TCRp V6-3*01, or a variant thereof. In some embodiments, TCRp V6 comprises TCRP V6-l*01, or a variant thereof. In some embodiments, TCRP V6 comprises TCRP V6-5*01, or a variant thereof. In some embodiments, TCRP V6, e.g., TCRp V6-5*01, is recognized, e.g., bound, by SEQ ID NO: 1 and / or SEQ ID NO: 2. In some embodiments, TCRP V6, e.g., TCRP V6-5*01, is recognized, e.g., bound, by SEQ ID NO: 9 and / or SEQ ID NO: 10. In some embodiments, TCRP V6 is recognized, e.g., bound, by SEQ ID NO: 9 and / or SEQ ID NO: 11. In some embodiments, TCRP V10 subfamily is also known as TCRP V12. In some embodiments, the TCRP VI0 subfamily comprises: TCRP VI0-1 *01, TCRP VI0-1 *02, TCRP V10-3*01 or TCRp V10-2*01, or a variant thereof. In some embodiments, TCRP V12 subfamily is also known as TCRp V8.1. In some embodiments, the TCRp V12 subfamily comprises: TCRp V12-4*01, TCRp V12-3*01, or TCRP V12-5*01, or a variant thereof. In some embodiments, TCRP V12 is recognized, e.g., bound, by SEQ ID NO: 15 and / or SEQ ID NO: 16. In some embodiments, TCRP V12 is recognized, e.g., bound, by any one of SEQ ID NOs 23-25, and / or any one of SEQ ID NO: 26-30: In some embodiments, the TCRp V5 subfamily is chosen from: TCRp V5-5*O1, TCRP V5-6*01, TCRp V5-4*01, TCRp V5-8*01, TCRp V5-l*01, or a variant thereof. In some embodiments, the TCRp V7 subfamily comprises TCRP V7-7*01, TCRP V7-6*01, TCRp V7 -8*02, TCRp V7 -4*01, TCRp V7-2*02, TCRp V7-2*03, TCRp V7-2*01, TCRP V7-3*01, TCRP V7-9*03, or TCRp V7-9*01, or a variant thereof. In some embodiments, the TCRP VI1 subfamily comprises: TCRp VI1-1 *01, TCRp VI1 -2*01 or TCRP Vil-3 *01, or a variant thereof. In some embodiments, the TCRP V14 subfamily comprises TCRp ¥14*01, or a variant thereof. In some embodiments, the TCRP ¥16 subfamily comprises TCRP VI6*01, or a variant thereof. In some embodiments, the TCRP V18 subfamily comprises TCRp ¥18*01, or a variant thereof. In some embodiments, the TCRP V9 subfamily comprises TCRP V9*01 or TCRP V9*02, or a variant thereof. In some embodiments, the TCRP ¥13 subfamily comprises TCRP ¥13*01, or a variant thereof. In some embodiments, the TCRp ¥4 subfamily comprises TCRp ¥4-2*01, TCRP ¥4-3*01, or TCRP ¥4-1*01, or a variant thereof. In some embodiments, the TCRP ¥3 subfamily comprises TCRP ¥3-1*01, or a variant thereof. In some embodiments, the TCRP ¥2 subfamily comprises TCRP ¥2*01, or a variant thereof. In some embodiments, the TCRP ¥15 subfamily comprises TCRp ¥15*01, or a variant thereof. In some embodiments, the TCRp V30 subfamily comprises TCRP ¥30*01, or TCRP ¥30*02, or a variant thereof. In some embodiments, the TCRP ¥19 subfamily comprises TCRP ¥19*01, or TCRp ¥19*02, or a variant thereof. In some embodiments, the TCRp V27 subfamily comprises TCRp ¥27*01, or a variant thereof. In some embodiments, the TCRp V28 subfamily comprises TCRP ¥28*01, or a variant thereof. In some embodiments, the TCRp ¥24 subfamily comprises TCRP ¥24-1*01, or a variant thereof. In some embodiments, the TCRP ¥20 subfamily comprises TCRP ¥20-1*01, or TCRP ¥20-1*02, or a variant thereof. In some embodiments, the TCRp V25 subfamily comprises TCRP ¥25-1*01, or a variant thereof. In some embodiments, the TCRP ¥29 subfamily comprises TCRp ¥29-1*01, or a variant thereof. Table 8A: List of TCRpV subfamilies and subfamily members Reference in Fig. 3 Subfamily Subfamily members A TCRp V6 Also referred to as: TCR VB 13.1 TCRp V6-4*01, TCRp V6-4*02, TCRp V6-9*01, TCRp V6-8*01, TCRp V6-5*01, TCRp V6-6*02, TCRp V6-6*01, TCRp V6-2*01, TCRp V6-3*01 or TCRp V6-1*01. B TCRp VI0 Also referred to as: TCRP VI2 TCRp VI0-1 *01, TCRp VI0-1 *02, TCRp VI0-3*01 or TCRp V10-2*01 C TCRp V12 Also referred to as: TCRP V8.1 TCRp V12-4*01, TCRp V12-3*01, or TCRp V12-5*01 D TCRp V5 TCRp V5-5*01, TCRp V5-6*01, TCRp V5-4*01, TCRp V5-8*01, TCRp V5-l*01 E TCRp V7 TCRp V7-7*01, TCRp V7-6*01, TCRp V7 -8*02, TCRp V7 -4*01, TCRp V7-2*02, TCRp V7-2*03, TCRp V7-2*01, TCRp V7-3*01, TCRp V7-9*03, or TCRp V7-9*01 F TCRp Vil TCRp VI 1-1*01, TCRp VI 1-2*01 or TCRp VI1-3*01 G TCRp V14 TCRp V14*01 ri TCRp VI6 TCRp V16*01 I TCRp VI8 TCRP V18*01 J TCRp V9 TCRp V9*01 or TCRp V9*02 K TCRp VI3 TCRp VI3 *01 L TCRp V4 TCRp V4-2*01, TCRp V4-3*01, or TCRp V4-1*01 M TCRp V3 TCRp V3-l*01 N TCRp V2 TCRp V2*01 0 TCRp VI5 TCRp VI5*01 P TCRp V30 TCRp V30*01, or TCRp V30*02 Q TCRp VI9 TCRp VI9*01, or TCRp VI9*02 R TCRp V27 TCRp V27*01. S TCRp V28 TCRp V28*01. T TCRp V24 TCRp V24-l*01 U TCRp V20 TCRp V20-l*01, or TCRp V20-l*02 V TCRp V25 TCRp V25-1*01 w TCRp V29 TCRp V29-1*01 Table 8B: Additional TCRpV subfamilies Subfamily TCRp VI TCRp VI7 TCRp V21 TCRp V23 TCRp V26 The various TCRPV subfamilies and / or subfamily members can be expressed at different levels in individuals, e.g., healthy individuals, as disclosed in Kitaura K. et al (2016), BMC Immunology vol 17: 38, the entire contents of which are hereby incorporated by reference. For 5 example, TCRP V6-5 is represented in approximately 3-6% healthy donors. The representation of various TCRBV subfamilies and / or subfamily members can also be different in cancer cells. For example, TCRPV is present in about 3-6% of tumor infiltrating T cells irrespective of tumor type (see Li B. et al., Nature Genetics, 2016, vol :48(7) :725-32 the entire contents of which are hereby incorporated by references). Li et al., also disclose that 10 TCRP V6-5 is present at a high frequency in tumor cells. Exemplary amino acid sequences for TCRPV subfamily members can be found on the ImMunoGeneTics Information System website: http: / / www.imgt.org / , or in a similar resource. Table 9: Alignment of TCRBV amino acid sequences (SEQ ID NOS 3457-3639, respectively, in order of appearance) FR1-IMGT CDR1-IMGT FR2-IMGT CDR2-IMGT FR3-IMGT CDR3-IMGT (1-26 (27 -38) (39- 55) (56- 65) (66 104) (105-117) Gene A B BC c C' c C" C D E F FG (1-15) (16-26) (27 -38) (39-46) (47-55) (56- 65) ¢66-74) (75-84) (85-96) (97-104) -------------------> -------------> --------> ----------> ----------> ------------> --------------> ---------> 1 10 15 16 23 26 27 38 3941 46 47 55 56 65 66 74 75 84 85 89 96 97 104 105 1........1 - - 1 1 . . . . . . 1 - - 1 1..........1 1 - 1 . . . . 1 1 .......1 1........1 1,......1 I........I I . . . I......1 | . . . . . . | |..... TRBV1 DTGITQTPKYLVTAM GSKRTMKREHL GH. . . . . . . DS MYWYRQKA KKSLEFMFY YNC. . . KEF IENKTVP.N HFTPECP.DS SRLYLHWALQQ EDSAAYLC TSSQ TRBV2 EPEVTQTPSHQVTQM GQEVILRCVPI SNH. . . . . . LY FYWYRQIL GQKVEFLVS FYN. . . NEI SEKSEIFDD QFSVERP.DG SNFTLKIRSTKL EDSAMYFC ASSE TRBV3-1 DTAVSQT P KYL' / TQM GNDKSIKCEQN LGH. . . . . . DT MYWYKQDS KKFLKIMFS YNN. . . KEL IINETVP.N RFSPKSP.DK AHLNLHINSLEL GDSAVYFC ASSQ TRBV3-2 DTAVSQT P KYLVTQM GKKESLK*EQN LGH. . . . . . NA MYWYKQDS KKFLKTMFI YSN. . . KEP ILNETVP.N rfspdsp.dk AHLNLHINSLEL GDSAVYFC ASSQ TRBV4-1 DT EVTQT P KHLVMGM TNKKSLKCEQH MGH. . . . . . RA MYWYKQKA KKPPELMFV YSY. . . EKL SINESVP.S RFSPECP.NS SLLNLHLHALQP EDSALYLC ASSQ TRBV4-2 ET GVTQT P RHLVMGM TNKKSLKCEQH LGH. . . . . . NA MYWYKQSA KKPLELMFV YNF. . . KEQ TENNSVP.S RFSPECP.NS SHLFLHLHTLQP EDSALYLC ASSQ TRBV4-3 ET GVTQT P RHLVMGM TNKKSLKCEQH LGH. . . . . . NA MYWYKQSA KKPLELMFV YSL. . . EER VENNSVP.S RFSPECP.NS SHLFLHLHTLQP EDSALYLC ASSQ TRBV5-1 KAGVTQTPRYLIKTR GQQVTLSCSPI SGH. . . . . . RS VSWYQQTP GQGLQFLFE YFS. . • ETQ RNKGNFP.G RFSGRQF.SN SRSEMNVSTLEL GDSALYLC ASSL TRBV5-3 EAGVTQSPTHLIKTR GQQVTLRCSPI SGH. . . . . . SS VSWYQQAP GQGPQFIFE YAN. . . ELR RSEGNFP.N RFSGRQF.HD CCSEMNVSALEL GDSALYLC ARSL TRBV5-4 ETGVTQSPTHLIKTR GQQVTLRCSSQ SGH. . . . . . NT VSWYQQAL GQGPQFIFQ YYR. . . EEE NGRGNFP.P RFSGLQF.PN YSSELNVNALEL DDSALYLC ASSL TRBV5-5 DAGVTQSPTHLIKTR GQQVTLRCSPI SGH. . . . . . KS VSWYQQVL GQGPQFIFQ YYE. . . KEE RGRGNFP.D RFSARQF.PN YSSELNVNALLL GDSALYLC ASSL TRBV5-6 DAGVTQSPTHLIKTR GQQVTLRCSPK SGH. . . . . . DT VSWYQQAL GQGPQFIFQ YYE. . EEE RQRGNFP.D RFSGHQF.PN YSSELNVNALLL GDSALYLC ASSL TRBV5-7 DAGVTQSPTHLIKTR GQHVTLRCSPI SGH. . . . . . TS VSSYQQAL GQGPQFIFQ YYE. . . KEE RGRGNFP.D QFSGHQF.PN YSSELNVNALLL GDSALYLC ASSL TRBV5-8 EAGVTQSPTHLIKTR GQQATLRCSPI SGH. . . . . . TS VYWYQQAL GLGLQFLLW YDE. . . GEE RNRGNFP.P RFSGRQF.PN YSSELNVNALEL EDSALYLC ASSL TRBV6-1 NAGVTQT P KFQVLKT GQSMTLQCAQD MNH. . . . . . NS MYWYRQDP GMGLRLIYY SAS. . . EGT TDKGEVP.N GYNVSRL.NK REFSLRLESAAP SQTSVYFC ASSE TRBV6-2 NAGVTQTPKFRVLKT GQSMTLLCAQD MNH. . . . . . EY MYWYRQDP GMGLRLIHY SVG. . . EGT TAKGEVP.D GYNVSRL. KK QNFLLGLESAAP SQTSVYFC ASSY TRBV6-3 NAGVTQTPKFRVLKT GQSMTLLCAQD MNH. . . . . . EY MYWYRQDP GMGLRLIHY SVG. . . EGT TAKGEVP.D GYNVSRL.KK QNFLLGLESAAP SQTSVYFC ASSY TRBV6-4 IAGITQAPTSQILAA GRRMTLRCTQD MRH. . . . . . NA MYWYRQDL GLGLRLIHY SNT. . . AGT TGKGEVP.D GYSVSRA.NT DDFPLTLASAVP SQTSVYFC ASSD TRBV6-5 NAGVTQT P KFQVLKT GQSMTLQCAQD MNH. . . . . . EY MSWYRQDP GMGLRLIHY SVG. . . AGI TDQGEVP.N GYNVSRS.TT EDFPLRLLSAAP SQTSVYFC ASSY TRBV6-6 NAGVTQTPKFRILKI GQSMTLQCTQD MNH. . . . . . NY MYWYRQDP GMGLKLIYY SVG. . .AGI TDKGEVP.N GYNVSRS.TT EDFPLRLEIAAP SQTSVYFC ASSY TRBV6-7 NAGVTQT P KFHVLKT GQSMTLLCAQD MNH. . . . . . EY MYRYRQDP GKGLRLIYY SVA. . . AAL TDKGEVP.N GYNVSRS.NT EDFPLKLESAAP SQTSVYFC ASSY TRBV6-8 NAGVTQTPKFHILKT GQSMTLQCAQD MNH. . . . . . GY MSWYRQDP GMGLRLIYY SAA. . .AGT TDK.EVP.N GYNVSRL.NT EDFPLRLVSAAP SQTSVYLC ASSY TRBV6-9 NAGVTQTPKFHILKT GQSMTLQCAQD MNH. . . . . . GY LSWYRQDP GMGLRRIHY SVA. . .AGI TDKGEVP.D GYNVSRS.NT EDFPLRLESAAP SQTSVYFC ASSY TRBV7-1 GAG VS Q S L RH KVAKK GKDVALRYDPI SGH. . . . . . NA LYWYRQSL GQGLEFPIY FQG. . . KDA ADKSGLPRD RFSAQRS. EG SISTLKFQRTQQ GDLAVYLC ASSS TRBV7-2 GAGVS Q S P S N KVT EK GKDVELRCDPI SGH. . . . . . TA LYWYRQSL GQGLEFLIY FQG. . . NSA PDKSGLPSD RFSAERT.GG SVSTLTIQRTQQ EDSAVYLC ASSL TRBV7-3 GAGVS QT P S N KVT EK GKYVELRCDPI SGH. . . . . . TA LYWYRQSL GQGPEFLIY FQG. . . TGA ADDSGLPND RFFAVRP. EG SVSTLKIQRTER GDSAVYLC ASSL TRBV7-4 GAGVS Q S P RY KVAK R GRDVALRCDSI SGH. . . . . . VT LYWYRQTL GQGSEVLTY SQS. . . DAQ RDKSGRPSG RFSAERP. ER SVSTLKIQRTEQ GDSAWLC ASSL TRBV7-6 GAGVS Q S P RY KVT KR GQDVALRCDPI SGH. . . . . . VS LYWYRQAL GQGPEFLTY FNY. . . EAQ QDKSGLPND RFSAERP. EG SI^TLTIQRTEQ RDSAMYRC ASSL TRBV7-7 GAGVS Q S P RY KVT KR GQDVTLRCDPI SSH. . . . . . AT LYWYQQAL GQGPEFLTY FNY. . . EAQ PDKSGLPSD RFSAERP.EG SISTLTIQRTEQ RDSAMYRC ASSL TRBV7-8 GAGVS Q S P RY KVAKR GQDVALRCDPI SGH. . . . . . VS LFWYQQAL GQGPEFLTY FQN. . .EAQ LDKSGLPSD RFFAERP. EG SVSTLKIQRTQQ EDSAVYLC ASSL TRBV7-9 DTGVSQNPRHKITKR GQNVTFRCDPI SEH. . . . . . NR LYWYRQTL GQGPEFLTY FQN. . .EAQ LEKSRLLSD RFSAERP. KG SFSTLEIQRTEQ GDSAMYLC ASSL TRBV9 DSGVTQTPKHLITAT GQRVTLRCSPR SGD. . . . . . LS VYWYQQSL DQGLQFLIQ YYN. . . GEE RAKGNIL.E RFSAQQF.PD LHSELNLSSLEL GDSALYFC AS SV TRBV10-1 DAEITQSPRHKITET GRQVTLACHQT WNH. . . . . . NN MFWYRQDL GHGLRLIHY SYG. . . VQD TNKGEVS.D GYSVSRS.NT EDLFLTLESAAS SQTSVYFC ASSE TRBV10-2 DAGITQSPRYKITET GRQVTLMCHQT WSH. . . . . . SY MFWYRQDL GHGLRLIYY SAA. . .ADI TDKGEVP.D GYWSRS . KT ENFPLTLESATR SQTSVYFC ASSE TRBV10-3 DAGITQSPRHKVTET GTPVTLRCHQT ENH. . . . . . RY MYWYRQDP GHGLRLIHY SYG. . . VKD TDKGEVS.D GYSVSRS.KT EDFLLTLESATS SQTSVYFC AISE TRBV11-1 EAEVAQ S P RY KIIEK SQAVAFWCDPI SGH. . . . . . AT LYWYRQIL GQGPELLVQ FQD. . . ESV VDDSQLPKD RFSAERL.KG VDSTLKIQPAEL GDSAMYLC ASSL TRBV11-2 EAGVAQSPRYKIIEK RQSVAFWCNPI SGH. . . . . . AT LYWYQQIL GQGPKLLIQ FQN. . . NGV VDDSQLPKD RFSAERL.KG VDSTLKIQPAKL EDSAVYLC ASSL TRBV11^3 EAGWQSPRYKIIEK KQPVAFWCNPI SGH... . . . . NT LYWYLQNL GQGPELLIR YEN. . . EEA VDDSQLPKD RFSAERL.KG VDSTLKIQPAEL GDSAVYLC ASSL TRBV12-1 DAG VIQ S P RH KVT EM GQSVTLRCEPI SGH... . . . .ND LLWYRQTF VQGLELLNY FCS. . . WTL VDDSGVSKD * FSAQMP.DV SFSTLRIQPMEP RDLGLYFC ASSF TRBV12-2 DAG11QSPKHE VT EM GQTVTLRCEPI FGH... . . . .NF LFWYRDTF VQGLELLSY FRS. . . *SI IDNAGMPTE RFSAERP.DG SFSTLKIQPAEQ GDSAVYVC ASRL TRBV12-3 DAG VIQ S P RH EVI EM GQEVTLRCKPI SGH... . . . .NS LFWYRQTM MRGLELLIY FNN. . . NVP IDDSGMPED RFSAKMP. NA SFSTLKIQPSEP RDSAVYFC ASSL TRBV12-4 DAG VIQ S P RH E VT EM GQEVTLRCKPI SGH... . . . . DY LFWYRQTM MRGLELLIY FNN. . . NVP IDDSGMPED RFSAKMP. NA SFSTLKIQPSEP RDSAVYFC ASSL TRBV12-5 DARVT QT P RH K. VT EM GQEVTMRCQPI LGH... . . . . NT VFWYRQTM MQGLELLAY FRN. . . RAP LDDSGMPKD RFSAEMP. DA TLATLKIQPSEP RDSAVYFC ASGL TRBV13 AAGVIQSPRHLIKEK RETATLKCYPI PRH... . . . .DT VYWYQQGP GQDPQFLIS FYE . KMQ SDKGSIP.D RFSAQQF.SD YHSELNMSSLEL GDSALYFC ASSL TRBV14 EAGVTQFPSHSVIEK GQTVTLRCDPI SGH... ....DN LYWYRRVM GKEIKFLLH FVK. . . ESK QDESGMPNN RFLAERT . GG TYSTLKVQPAEL EDSGVYFC ASSQ TRBV15 DAMVIQNP RYQ VTQF GKPVTLSCSQT LNH... . . . . NV MYWYQQKS SQAPKLLFH YYD. . . KDF NNEADTP.D NFQSRRP.NT SFCFLDIRSPGL GDTAMYLC AT SR TRBV16 GEEVAQTPKHLVRGE GQKAKLYCAPI KGH... . . . .SY VFWYQQVL KNEFKFLIS FQN... . ENV FDETGMPKE RFSAKCL.PN SPCSLEIQATKL EDSAVYFC ASSQ TRBV17 E P G VS QT P RH K VTNM GQEVILRCDPS SGH... ....MF VHWYRQNL RQEMKLLIS FQY... .QNI AVDSGMPKE RFTAERP. NG TSSTLKIHPAEP RDSAVYLY SSG TRBV18 NAGVMQNPRHLVRRR GQEARLRCSPM KGH... ....SH VYWYRQLP EEGLKFMVY LQK. . . ENI IDESGMPKE RFSAEFP. KE GPSILRIQQWR GDSAAYFC ASSP TRBV19 DGGITQSPKYLFRKE GQNVTLSCEQN LNH... . . . . DA MYWYRQDP GQGLRLIYY SQI... . VND FQKGDIA.E GYSVSRE.KK ESFPLTVTSAQK NPTAFYLC ASSI TRBV20-1 GAWSQHPSWVICKS GTSVKIECRSL DFQ... . . .ATT MFWYRQFP KQS LMLMAT SNEG. . SKA TYEQGVEKD KFLINHA.SL TLSTLTVTSAHP EDSSFYIC SAR TRBV21^1 DTKVTQRPRLLVKAS EQKAKMDCVPI KAH. . . . . . . SY VYWYRKKL EEELKFLVY FQN. . . EEL IQKAEIINE RFLAQCS.KN SSCTLEIQSTES GDTALYFC ASSK TRBV23^1 HAKVTQTPGHLVKGK GQKTKMDCTPE KGH... ....TF VYWYQQNQ NKEFMLLIS FQN. . - EQV LQETEMHKK RFSSQCP.KN APCSLAILSSEP GDTALYLC ASSQ TRBV24-1 DADVTQTPRNRITKT GKRIMLECSQT KGH... . . . . DR MYWYRQDP GLGLRLIYY SFD. . . VKD INKGEIS.D GYSVSRQ.AQ AKFSLSLESAIP NQTALYFC ATSDL TRBV25-1 EADIYQT P RYLVIGT GKKITLECSQT MGH... . . . .DK MYWYQQDP GMELHLIHY SYG. . . VNS TEKGDLS.S EST VS RI. RT EHFPLTLESARP SHTSQYLC ASSE TRBV2 6 DAVVT Q F P RH RI I GT GKEFILQCSQN MNH... ....VT MYWYRQDP GLGLKLVYY SPG. . .TGS TEKGDIS.E GYHVS*N.TI ASFPLTLKSAST NQTSVYLY ASSS TRBV27 EAQVTQNPRYLITVT GKKLTVTCSQN MNH... ....EY MSWYRQDP GLGLRQIYY SMN. . . VEV TDKGDVP.E GYKVSRK.EK RNFPLILESPSP NQTSLYFC ASSL TRBV28 D VKVT Q S S R Y L VKRT GEKVFLECVQD MDH... ....EN MFWYRQDP GLGLRLIYF SYD. . . VKM KEKGDIP.E GYSVSRE.KK ERFSLILESAST NQTSMYLC ASSL TRBV29-1 SAVISQKPSRDICQR GTSLTIQCQVD SQV... .... TH MFWYRQQP GQSLTLIAT ANQG. . SEA TYESGFVID KFPISRP.NL TFSTLTVSNMSP EDSSIYLC SVE TRBV30 SQTIHQWPATLVQPV GSPLSLECTVE GTS... ...NPN LYWYRQAA GRGLQLLFY SVG. . . . IG QISSEVP.Q NLSASRP.QD RQFILSSKKLLL SDSGFYLC AWS The alignment of TCRBV amino acid sequences in Table 9 underscores the diversity of TCR sequences. In particular, the TRBV sequences from different subfamilies are considerably different from each other. Anti-TCRpV antibodies Disclosed herein, is the discovery of a novel class of antibodies, i.e. anti-TCRpV antibody molecules disclosed herein, which despite having low sequence similarity (e.g., low sequence identity among the different antibody molecules that recognize different TCRPV subfamilies), recognize a structurally conserved region, e.g., domain, on the TCRPV protein (e.g., as denoted by the circled area in FIG. 24A) and have a similar function (e.g., a similar cytokine profile). Thus, the anti-TCRpV antibody molecules disclosed herein share a structurefunction relationship. Without wishing to be bound by theory, it is believed that in some embodiments, the anti-TCRpV antibody molecules disclosed herein bind to an outward facing epitope of a TCRpV protein when it is in a complex with a TCRalpha protein, e.g., as described by the circled area in FIG. 24A. In some embodiments, the anti-TCRpV antibody molecules disclosed herein recognize (e.g., bind to), a structurally conserved domain on the TCRPV protein (e.g., as denoted by the circled area in FIG. 24A). In some embodiments, the anti-TCRpV antibody molecules disclosed herein do not recognize, e.g., bind to, an interface of a TCRpV: TCRalpha complex. In some embodiments, the anti-TCRpV antibody molecules disclosed herein do not recognize, e.g., bind to, a constant region of a TCRPV protein. An exemplary antibody that binds to a constant region of a TCRBV region is JOVI. 1 as described in Viney el al., (Hybridoma. 1992 Dec; 11(6):701-13). In some embodiments, the anti-TCRpV antibody molecules disclosed herein do not recognize, e.g., bind to, one or more (e.g., all) of a complementarity determining region (e.g., CDR1, CDR2 and / or CDR3) of a TCRpV protein. In some embodiments, the anti-TCRpV antibody molecules disclosed herein binds (e.g., specifically binds) to a TCRpV region. In some embodiments, binding of anti-TCRpV antibody molecules disclosed herein results in a cytokine profile that differs from a cytokine profile of a T cell engager that binds to a receptor or molecule other than a TCRPV region (“a non-TCRpV-binding T cell engager”). In some embodiments, the non-TCRpV-binding T cell engager comprises an antibody that binds to a CD3 molecule (e.g., CD3 epsilon (CD3e) molecule); or a TCR alpha (TCRa) molecule. In some embodiments, the non-TCRpV-binding T cell engager is an OKT3 antibody or an SP34-2 antibody. In an aspect, the disclosure provides an anti-TCRpV antibody molecule that binds to human TCRPV, e.g, a TCRPV gene family, e.g., one or more of a TCRPV subfamily, e.g., as described herein, e.g, in FIG. 3, Table 8A, or Table 8B. In some embodiments, the anti-TCRpV antibody molecule binds to one or more TCRPV subfamilies chosen from: a TCRp V6 subfamily, a TCRP V10 subfamily, a TCRP V12 subfamily, a TCRP V5 subfamily, a TCRP V7 subfamily, a TCRp Vil subfamily, a TCRp VI4 subfamily, a TCRp VI6 subfamily, a TCRp VI8 subfamily, a TCRP V9 subfamily, a TCRP VI3 subfamily, a TCRP V4 subfamily, a TCRP V3 subfamily, a TCRp V2 subfamily, a TCRp VI5 subfamily, a TCRp V30 subfamily, a TCRp VI9 subfamily, a TCRP V27 subfamily, a TCRP V28 subfamily, a TCRP V24 subfamily, a TCRp V20 subfamily, TCRp V25 subfamily, a TCRp V29 subfamily, a TCRp VI subfamily, a TCRp VI7 subfamily, a TCRp V21 subfamily, a TCRp V23 subfamily, or a TCRp V26 subfamily, or a variant thereof. In some embodiments, the anti-TCRpV antibody molecule binds to a TCRP V6 subfamily comprising: TCRp V6-4*01, TCRp V6-4*02, TCRp V6-9*01, TCRp V6-8*01, TCRp V6-5*01, TCRp V6-6*02, TCRp V6-6*01, TCRp V6-2*01, TCRp V6-3*01 or TCRp V6-l*01, or a variant thereof. In some embodiments the TCRp V6 subfamily comprises TCRp V6-5*01, or a variant thereof. In some embodiments, TCRP V6 comprises TCRp V6-4*01, or a variant thereof. In some embodiments, TCRP V6 comprises TCRP V6-4*02, or a variant thereof. In some embodiments, TCRP V6 comprises TCRp V6-9*01, or a variant thereof. In some embodiments, TCRp V6 comprises TCRP V6-8*01, or a variant thereof. In some embodiments, TCRp V6 comprises TCRp V6-5*01, or a variant thereof. In some embodiments, TCRp V6 comprises TCRp V6-6*02, or a variant thereof. In some embodiments, TCRp V6 comprises TCRp V6-6*01, or a variant thereof. In some embodiments, TCRp V6 comprises TCRp V6-2*01, or a variant thereof. In some embodiments, TCRP V6 comprises TCRP V6-3*01, or a variant thereof. In some embodiments, TCRP V6 comprises TCRP V6-l*01, or a variant thereof. In some embodiments, the anti-TCRpV antibody molecule binds to a TCRp VI0 subfamily comprising: TCRp V10-1 *01, TCRp V10-l*02, TCRp V10-3*01 or TCRp VI0-2*01, or a variant thereof. In some embodiments, the anti-TCRpV antibody molecule binds to a TCRP V12 subfamily comprising: TCRP V12-4*01, TCRp V12-3*01 or TCRp V12-5*01, or a variant thereof. In some embodiments, the anti-TCRpV antibody molecule binds to a TCRP V5 subfamily comprising: TCRp V5-5*01, TCRp V5-6*01, TCRP V5-4*01, TCRp V5-8*01, TCRp V5-l*01, or a variant thereof. Exemplary anti-TCRpV antibody molecules and the corresponding TCRPV subfamily recognized by said anti-TCRpV antibody molecules is disclosed in Table 10A. Table 10A: Exemplary anti-TCRpV antibody molecules TRBV gene name TRBV allele name Reagents monoclonal antibodies Clone name and Specificity Company product Isotype | TRBV2 TRBV2*01 TRBV2*02 TRBV2*03 IsMMU 546 (TRBV2) Serotec V BETA 22 Coulter Vbeta22 Mouse IgGl TRBV3-1 TRBV3-P01 FIN9 (TRBV3-1) AM KB 1-2 (TRBV3-1) Serotec Vbeta9 Coulter Vbeta9 Mouse IgG2a |] Mouse IgGl 1 TRBV3-l*02 BD Biosciences Vbeta9 TRBV4-1 TRBV4-l*01 ZOE (TRBV4-1, TRBV4-2, TRBV4-3) 3G5 (TRBV4-1) Serotec V BETA 7 Coulter Vbeta7 Mouse IgG2a TRBV4-P02 Pierce EndogenV beta 7.1 Mouse IgG2b TRBV4-2 TRBV4-2*01 TRBV4-2*02 ZOE (TRBV4-I, TRBV4-2, TRBV4-3) Serotec V BETA 7 Coulter Vbeta7 Mouse IgG2a | TRBV4-3 TRBV4-3*01 TRBV4-3*02 TRBV4-3*03 ZOE (TRBV4-1, TRBV4- 2, TRBV4-3) Serotec V BETA 7 Coulter Vbeta7 Mouse IgG2a TRBV4-3*04 ZIZOU4 (TRBV4-3) Coulter Vbeta7.2 Mouse IgG2a [ TRBV5-1 TRBV5-l*01 IMMU157 (TRBV5-1) Serotec Vbeta5.1 Coulter Vbeta5.1 Mouse IgG2a TRBV5-l*02 LC4 (TRBV5-1) Pierce Endogen V beta 5(c) BD Biosciences Vbeta5(c) Mouse IgGl TRBV5-4 TRBV5-4*01 TRBV5-4*02 TRBV5-4*03 TRBV5-4*04 1 TRBV5-5 TRBV5-5*01 3D11 (TRBV5-5) 1C1 (TRBV5-5, TRBV5-6) Serotec VBETA5.3 Coulter Vbeta5.3 Mouse IgGl ] TRBV5-5*02 Pierce Endogen V beta 5(a) BD Biosciences Vbeta5(a) Mouse T 1 IgGl TRBV5-5*03 Pierce Endogen V beta Mouse ][ W112 (TRBV5-5) MH3-2 (TRBV5-5, TRBV5-6) 5(b) Serotec V beta 5.2 / 5.3 BD Biosciences Vbeta5(b) IgGl BD Biosciences Vbeta5 Mouse IgG2a 4H11 (TM27) as disclosed in U.S. Patent 5,861,155 । TRBV5-6 TRBV5-6*01 36213 (TRBV5-6) 1C1 (TRBV5-5, TRBV5-6) MH3-2 (TRBV5-5, TRBV5-6) Serotec Vbeta5.2 Mouse ]| IgGl J Mouse IgGl Mouse IgG2a ][ BD Biosciences Vbeta5(a) BD Biosciences Vbeta5 TRBV5-8 TRBV5-8*01 | TRBV5-8*02 TRBV6-1 TRBV6-l*01 BAM13 (TRBV6-1, TRBV6-5) Pierce Endogen V beta 13 BD Biosciences Vbetal3.1, 13.3 Mouse IgGl TRBV6-2 TRBV6-2*01 H132 Coulter Vbetal3.2 Mouse IgGl | TRBV6-3 TRBV6-3*01 1 TRBV6-4 TRBV6-4*01 1 TRBV6-4*02 TRBV6-5 TRBV6-5*01 IMMU 222 (TRBV6-5, TRBV6-6 and TRBV6-9) BAM13 (TRBV6-1, TRBV6-5) Serotec V BETA 13.1 Coulter Vbetal3.1 Mouse IgG2b Pierce Endogen V beta 13 BD Biosciences Vbetal3.1, 13.3 Mouse IgGl TRBV6-6 TRBV6-6*01 JU-74 (TRBV6-6) JU74.3 (TRBV6-6) IMMU 222 (TRBV6-5, TRBV6-6 and TRBV6-9) Serotec Vbetal3.6 Coulter Vb eta 13.6 Mouse IgGl TRBV6-6*02 TRBV6-6*03 TRBV6-6*04 Serotec V BETA 13.1 Coulter Vbetal3.1 Mouse IgG2b TRBV6-6*05 TRBV6-8 TRBV6-8*01 TRBV6-9 TRBV6-9*01 IMMU 222 (TRBV6-5, TRBV6-6 and TRBV6-9) Serotec V BETA 13.1 Coulter Vb eta 13.1 Mouse IgG2b _ ][ TRBV7-2 TRBV7-2*01 OT145 (TRBV7-2) Pierce Endogen V beta 6.7 BD Biosciences Vbeta6.7 Mouse IgGl TRBV7-2*02 TRBV7-2*03 TRBV7-2*04 TRBV7-3 TRBV7-3*01 । TRBV7-3*04 TRBV7-3*05 TRBV7-4 TRBV7-4*01 1 TRBV7-6 TRBV7-6*01 1 TRBV7-6*02 TRBV7-7 TRBV7-7*01 1 TRBV7-7*02 TRBV7-8 TRBV7-8*01 1 TRBV7-8*02 TRBV7-8*03 TRBV7-9 TRBV7-9*01 TRBV7-9*02 TRBV7-9*03 TRVB7-9*04 TRBV7-9*05 TRBV7-9*06 TRBV7-9*07 TRBV9 TRBV9*01 BL37.2 (TRBV9) Serotec Vbetal Coulter Vbetal Rat IgGl । TRBV9*02 TRBV9*03 TRBV10-1 TRBV10-2 TRBV10-l*01 S511 (TRBV10-1, TRBV10-2, TRBV10-3) Pierce Endogen V beta 12 BD Biosciences Vbetal2 Mouse IgG2b TRBV10-l*02 TRBV10-2*01 TRB VI 0-2*02 TRBV10-3 TRBV10-3*01 VER2.32.1 (TRBV10-3) S511 (TRBV10-1, TRBV10-2, TRBV10-3) Serotec Vbetal 2 Coulter Vbetal2 Mouse IgG2a TRBV10-3*02 TRBV10-3*03 Pierce Endogen V beta 12 BD Biosciences Vbetal2 Mouse IgG2b TRBV10-3*04 TRBV11-1 TRBVll-l*01 1 TRBV11-2 TRBV11-2*01 IG125 (TRBVI1-2) Serotec Vbeta21.3 Coulter Vbeta21.3 Mouse IgG2a TRBV11-2*02 TRBV11-2*03 TRBV11-3 TRBV11-3*01 _______1 TRBV11-3*02 । TRBV11-3*03 TRB¥ll-3*04 TRBV12-3 TRBV12-3*01 56C5 (TRBV12-3, TRBV12-4) 56C5.2 (TRBV12-3, TRBV12-4) 16G8 (TRBV12-3, TRBV12-4) MX-6 (TRBV12-3, TRBV12-4) JR2 (TRBV12-3, TRBV12-4, TRBV12-5) Serotec Vbeta8.1 / 8.2 Coulter Vbeta8 Mouse IgG2a TRBV12-4 TRBV12-4*01 Pierce Endogen V beta 8(a) BD Biosciences Vbeta8 Mouse IgG2b TRBV12-4*02 Pierce Endogen V beta 8(b) Mouse IgG2a BD Biosciences Vbeta8 Mouse IgG2b TRBV12-5 TRBV12-5*01 JR2 (TRBV12-3, TRBV12-4, TRBV12-5) BD Biosciences Vbeta8 Mouse IgG2b ][ TRBV13 TRBV13*01 AF-23 (TRBV13) AF23 (TRBV13) AHUT7 (Vbeta23) Serotec Vbeta23 Coulter Vbeta23 BD Biosciences Vbeta23 Mouse 1 IgGl TRBV13*02 TRBV14 TRBV14*01 TAMAYA1.2 (TRBV14) Serotec Vbetal6 Coulter Vbetal6 Mouse IgGl ][ TRBV14*02 TRBV15 TRBV15*01 । TRBV15*02 TRBV15*03 TRBV16 TRBV16*01 | TRBV16*03 TRBV18 TRBV18*01 BA62 (TRBV18) BA62.6 (TRBV18) Serotec V BETA 18 Coulter Vbetal8 Mouse IgGl ][ TRBV19 TRBV19*01 Cl (TRBV19) E17.5F3 (TRBV19) E17.5F3.15.13 (TRBV19) Pierce Endogen V beta 17 BD Biosciences Vbetal7 Mouse IgGl TRBV19*02 Serotec Vbetal7 Coulter Vbetal7 Mouse IgGl TRBV19*03 TRBV20-1 TRBV20-l*01 MPB2D5 (TRBV20-1) Serotec VBETA2 Coulter Vbeta2 Mouse IgGl TRBV20-l*02 TRBV20-l*03 TRBV20-l*04 TRBV20-l*05 TRBV20-l*06 TRBV20-l*07 TRBV24-1 TRBV24-l*01 TRBV25-1 TRBV25-l*01 C21 (TRBV25-1) Serotec V BETA 11 Coulter Vbetal 1 Mouse IgG2a TRBV27 TRBV27*01 CAS1.1.3 (TRBV27) Serotec Vbetal4 Coulter Vbetal4 Mouse IgGl TRBV28 TRBV28*01 CH92 (TRBV28) 8F10 (TRBV28) JOVI-3 (TRBV28) Serotec Vbeta3 Coulter Vbeta3 Mouse IgM Pierce Endogen V beta 3.1 BD Biosciences Vbeta3 Mouse IgGl Mouse IgG2a TRBV29-1 TRBV29-l*01 WJF24 Coulter Vbeta4 Rat IgM TRBV29-l*02 TRBV29-l*03 TRBV30 TRBV30*01 ELL1.4 (TRBV30) Serotec Vbeta20 Coulter Vbeta20 Mouse IgGl TRBV30*02 TRBV30*04 TRBV30*05 In some embodiments, the anti-TCRpV antibody molecule does not bind to TCRp VI2, or binds to TCRp V12 with an affinity and / or binding specificity that is less than (e.g., less than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity 5 and / or binding specificity of the 16G8 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments, the anti-TCRpV antibody molecule binds to TCRP V12 with an affinity and / or binding specificity that is greater than (e.g., greater than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding 10 specificity of the 16G8 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments, the anti-TCRpV antibody molecule binds to a TCRPV region other than TCRP ¥12 (e.g., TCRPV region as described herein, e.g., TCRP V6 subfamily (e.g., TCRP V6-5*01) with an affinity and / or binding specificity that is greater than (e.g., greater than 15 about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the 16G8 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments, the anti-TCRP¥ antibody molecule does not bind to TCRP ¥5-5*01 or TCRP ¥5-1*01, or binds to TCRp V5-5*01 or TCRp V5-l*01 with an affinity and / or binding specificity that is less than (e.g., less than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the TM23 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments, the anti-TCRpV antibody molecule binds to TCRp ¥5-5*01 or TCRP V5-l*01with an affinity and / or binding specificity that is greater than (e.g., greater than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the TM23 murine antibody or a humanized version thereof as described in US Patent 5,861,155. In some embodiments, the anti-TCRpV antibody molecule binds to a TCRpV region other than TCRP V5-5*01 or TCRp V5-l*01 (e.g., TCRPV region as described herein, e.g., TCRP ¥6 subfamily (e.g., TCRP V6-5*01) with an affinity and / or binding specificity that is greater than (e.g, greater than about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or about 2-, 5-, or 10- fold) the affinity and / or binding specificity of the TM23 murine antibody or a humanized version thereof as described in US Patent 5,861,155. Anti-TCRp V6 antibodies Accordingly, in one aspect, the disclosure provides an anti-TCRpV antibody molecule that binds to human TCRP V6, e.g., a TCRp V6 subfamily comprising: TCRP ¥6-4*01, TCRP ¥6-4*02, TCRP ¥6-9*01, TCRp ¥6-8*01, TCRp ¥6-5*01, TCRp ¥6-6*02, TCRp ¥6-6*01, TCRp ¥6-2*01, TCRp ¥6-3*01 or TCRp V6-1 *01. In some embodiments the TCRp ¥6 subfamily comprises TCRP V6-5*01 or a variant thereof. In some embodiments, TCRp V6 comprises TCRp V6-4*01, or a variant thereof In some embodiments, TCRP ¥6 comprises TCRP V6-4*02, or a variant thereof. In some embodiments, TCRP ¥6 comprises TCRP ¥6-9*01, or a variant thereof. In some embodiments, TCRp ¥6 comprises TCRp ¥6-8*01, or a variant thereof. In some embodiments, TCRp ¥6 comprises TCRP ¥6-5*01, or a variant thereof. In some embodiments, TCRp ¥6 comprises TCRp ¥6-6*02, or a variant thereof. In some embodiments, TCRP ¥6 comprises TCRP ¥6-6*01, or a variant thereof. In some embodiments, TCRP ¥6 comprises TCRp ¥6-2*01, or a variant thereof. In some embodiments, TCRP ¥6 comprises TCRP ¥6-3*01, or a variant thereof. In some embodiments, TCRp ¥6 comprises TCRP ¥6-1*01, or a variant thereof. In some embodiments, TCRp ¥6-5*01 is encoded by the nucleic acid sequence of SEQ ID NO: 43, or a sequence having 85%, 90%, 95%, 99% or more identity thereof. SEQIDNO: 43 ATGAGCATCGGCCTCCTGTGCTGTGCAGCCTTGTCTCTCCTGTGGGCAGGTCCAGTG AATGCTGGTGTCACTCAGACCCCAAAATTCCAGGTCCTGAAGACAGGACAGAGCAT G AC AC T GC AGTGTGC C C AGGAT ATGA AC C ATGA AT AC ATGT C C TGGT ATC G AC A AG ACCCAGGCATGGGGCTGAGGCTGATTCATTACTCAGTTGGTGCTGGTATCACTGACC AAGGAGAAGTCCCCAATGGCTACAATGTCTCCAGATCAACCACAGAGGATTTCCCG CTCAGGCTGCTGTCGGCTGCTCCCTCCCAGACATCTGTGTACTTCTGTGCCAGCAGT TACTC In some embodiments, TCRp V6-5*01 comprises the amino acid sequence of SEQ ID NO: 44, or an amino acid sequence having 85%, 90%, 95%, 99% or more identity thereof. SEQIDNO: 44 MSIGLLCCAALSLLWAGPVNAGVTQTPKFQVLKTGQSMTLQCAQDMNHEYMSWYRQ DPGMGLRLIHYSVGAGITDQGEVPNGYNVSRSTTEDFPLRLLSAAPSQTSVYFCASSY In some embodiments, the anti-TCRpV antibody molecule, e.g., anti-TCRp V6 (e.g., anti-TCRp V6-5*01) antibody molecule, is a non-murine antibody molecule, e.g., a human or humanized antibody molecule. In some embodiments, the anti-TCRpV antibody molecule, e.g., anti-TCRp V6 (e.g., anti-TCRp V6-5*01) antibody molecule is a human antibody molecule. In some embodiments, the anti-TCRpV antibody molecule, e.g., anti-TCRp V6 (e.g., anti-TCRp V6-5*01) antibody molecule is a humanized antibody molecule. In some embodiments, the anti-TCRpV antibody molecule, e.g., anti-TCRpV6(e.g., anti-TCRp V6-5*01) antibody molecule, is isolated or recombinant. In some embodiments, the anti-TCRpV antibody molecule, e.g., anti-TCRp V6 (e.g., anti-TCRp V6-5*01) antibody molecule, comprises at least one antigen-binding region, e.g., a variable region or an antigen-binding fragment thereof, from an antibody described herein, e.g., an antibody chosen from any one of A-H. 1 to A-H.85, e.g., A-H. 1, A-H.2 or A-H.68, or an antibody described in Table 1, or encoded by a nucleotide sequence in Table 1, or a sequence substantially identical (e.g., at least 80%, 85%, 90%, 92%, 95%, 97%, 98%, 99% or higher identical) to any of the aforesaid sequences. In some embodiments, the anti-TCRpV antibody molecule, e.g., anti-TCRp V6 (e.g., anti-TCRp V6-5*01) antibody molecule, comprises at least one, two, three or four variable regions from an antibody described herein, e.g., an antibody chosen from any one of A-H.l to 115 A-H.85, e.g., A-H. 1, A-H.2 or A-H.68, or an antibody described in Table 1, or encoded by a nucleotide sequence in Table 1, or a sequence substantially identical (e.g., at least 80%, 85%, 90%, 92%, 95%, 97%, 98%, 99% or higher identical) to any of the aforesaid sequences. In some embodiments, the anti-TCRpV antibody molecule, e.g., anti-TCRp V6 (e.g., anti-TCRp V6-5*01) antibody molecule, comprises at least one or two heavy chain variable regions from an antibody described herein, e.g., an antibody chosen from any one of A-H.l to A-H.85, e.g., A-H.l, A-H.2 or A-H.68, or an antibody molecule described in Table 1, or encoded by a nucleotide sequence in Table 1, or a sequence substantially identical (e.g., at least 80%, 85%, 90%, 92%, 95%, 97%, 98%, 99% or higher identical) to any of the aforesaid sequences. In some embodiments, the anti-TCRpV antibody molecule comprises a heavy chain variable region (VH) having a consensus sequence of SEQ ID NO: 231 or 3290. In some embodiments, the anti-TCRpV antibody molecule, e.g., anti-TCRp V6 (e.g., anti-TCRp V6-5*01) antibody molecule, comprises at least one or two light chain variable regions from an antibody described herein, e.g., an antibody chosen from any one of A-H.l to A-H.85, e.g., A-H.l, A-H.2 or A-H.68, or an antibody described in Table 1, or encoded by a nucleotide sequence in Table 1, or a sequence substantially identical (e.g., at least 80%, 85%, 90%, 92%, 95%, 97%, 98%, 99% or higher identical) to any of the aforesaid sequences. In some embodiments, the anti-TCRpV antibody molecule comprises a light chain variable region (VL) having a consensus sequence of SEQ ID NO: 230 or 3289. In some embodiments, the anti-TCRpV antibody molecule, e.g., anti-TCRp V6 (e.g., anti-TCRp V6-5*01) antibody molecule, comprises a heavy chain constant region for an IgG4, e.g., a human IgG4. In still another embodiment, the anti-TCRpV antibody molecule, e.g., anti-TCRp V6 (e.g., anti-TCRp V6-5*01) antibody molecule includes a heavy chain constant region for an IgGl, e.g., a human IgGl. In one embodiment, the heavy chain constant region comprises an amino sequence set forth in Table 3, or a sequence substantially identical (e.g., at least 80%, 85%, 90%, 92%, 95%, 97%, 98%, 99% or higher identical) thereto. In some embodiments, the anti-TCRpV antibody molecule, e.g., anti-TCRp V6 (e.g., anti-TCRp V6-5*01) antibody molecule, includes a kappa light chain constant region, e.g., a human kappa light chain constant region. In one embodiment, the light chain constant region comprises an amino sequence set forth in Table 3, or a sequence substantially identical (e.g., at least 80%, 85%, 90%, 92%, 95%, 97%, 98%, 99% or higher identical) thereto. In some embodiments, the anti-TCRpV antibody molecule, e.g., anti-TCRp V6 (e.g., anti-TCRp V6-5*01) antibody molecule, includes at least one, two, or three complementarity determining regions (CDRs) from a heavy chain variable region (VH) of an antibody described 116 herein, e.g., an antibody chosen from any one of A-H. 1 to A-H.85, e.g., A-H.l, A-H.2 or A-H.68, or an antibody described in Table 1, or encoded by a nucleotide sequence in Table 1, or a sequence substantially identical (e.g., at least 80%, 85%, 90%, 92%, 95%, 97%, 98%, 99% or higher identical) to any of the aforesaid sequences. In some embodiments, the anti-TCRpV antibody molecule, e.g., anti-TCRp V6 (e.g., anti-TCRp V6-5*01) antibody molecule, includes at least one, two, or three CDRs (or collectively all of the CDRs) from a heavy chain variable region comprising an amino acid sequence shown in Table 1, or encoded by a nucleotide sequence shown in Table 1. In one embodiment, one or more of the CDRs (or collectively all of the CDRs) have one, two, three, four, five, six or more changes, e.g., amino acid substitutions or deletions, relative to the amino acid sequence shown in Table 1, or encoded by a nucleotide sequence shown in Table 1. In some embodiments, the anti-TCRpV antibody molecule, e.g., anti-TCRp V6 (e.g., anti-TCRp V6-5*01) antibody molecule, includes at least one, two, or three complementarity determining regions (CDRs) from a light chain variable region of an antibody described herein, e.g., an antibody chosen from a...

Claims

30 05 251. A composition comprising a molecule that comprises an antigen binding domain that binds to a T cell receptor beta variable (TCRPV) region, wherein the antigen binding domain that binds to a TCRPV region comprises (i) a heavy chain variable region (VH) comprising a heavy chain complementarity determining region 1 (HC CDR1) comprising the sequence GHDFRLTYIH (amino acids 26-35 of SEQ ID NO: 1346), a heavy chain complementarity determining region 2 (HC CDR2) comprising the sequence RVSAGSGNVKYNEKFKG (ammo acids 50-66 of SEQ ID NO: 1346), and a heavy chain complementarity determining region 3 (HC CDR3) comprising the sequence SYYSYDVLDY (SEQ ID NO: 47), and (ii) a light chain variable region (VL) comprising a light chain complementarity determining region 1 (LC CDR1) comprising the sequence KASQNVADRW (ammo acids 24-34 of SEQ ID NO: 1349), a light chain complementarity determining region 2 (LC CDR2) comprising the sequence SSSHRYK (amino acids 50-56 of SEQ ID NO: 1349), and a light chain complementarity determining region 3 (LC CDR3) comprising the sequence QQFKSYPLT (SEQ ID NO: 53).

2. The composition of claim 1, wherein:(i) the VH of the antigen binding domain that binds to a TCRPV region comprises a sequence having at least 80% sequence identity to the sequence of SEQ ID NO: 1346, and the VL of the antigen binding domain that binds to a TCRPV region comprises a sequence having at least 80% sequence identity to the sequence of SEQ ID NO: 1349;(ii) the VH of the antigen binding domain that binds to a TCRpV region comprises a sequence having at least 90% sequence identity to the sequence of SEQ ID NO: 1346, and the VL of the antigen binding domain that binds to a TCRPV region comprises a sequence having at least 90% sequence identity to the sequence of SEQ ID NO: 1349;(iii) the VH of the antigen binding domain that binds to a TCRPV region comprises a sequence having at least 95% sequence identity to the sequence of SEQ ID NO: 1346, and the VL of the antigen binding domain that binds to a TCRPV region comprises a sequence having at least 95% sequence identity to the sequence of SEQ ID NO: 1349; or30 05 25(iv) the VH of the antigen binding domain that binds to a TCRPV region comprises the sequence of SEQ ID NO: 1346, and the VL of the antigen binding domain that binds to a TCRPV region comprises the sequence of SEQ ID NO: 1349.

3. The composition of claim 1 or 2, wherein the antigen binding domain that binds to a TCRPV region is a Fab.

4. The composition of claim 1 or 2, wherein the antigen binding domain that binds to a TCRPV region is a single chain variable fragment (scFv).

5. The composition of claim 4, wherein the antigen binding domain that binds to a TCRPV region comprises the sequence of SEQ ID NO: 1331.

6. The composition of any one of claims 1-5, wherein the molecule comprises a heavy chain comprising the VH of the antigen binding domain that binds to a TCRPV region and a heavy chain constant region.

7. The composition of any one of claims 1 -6, wherein the molecule comprises a light chaincomprising the VL of the antigen binding domain that binds to a TCRPV region and a light chain constant region.

8. The composition of claim 7. wherein the light chain constant region is a kappa light chain constant region or a fragment thereof or a lambda light chain constant region or a fragment thereof.

9. The composition of claim 7 or 8, wherein the light chain constant region comprises the sequence of SEQ ID NO: 39.

10. The composition of any one of claims 1-9, wherein the molecule further comprises a cytokine.

11. The composition of claim 10, wherein the cytokine is selected from the group consisting of interleukin-2 (IL-2), interleukin-12 (IL-12), interleukin-15 (IL-15), interleukin-18 (IL-18), interleukin-21 (IL-21), interleukin-7 (IL-7), and interferon gamma.

12. The composition of claim 10 or 11, wherein the cytokine comprises IL-15, wherein the IL-15 comprises the sequence of SEQ ID NO: 2170, wherein the IL-15 is covalently linked to an IL15Ralpha dimerizing domain.

13. The composition of claim 12, wherein the IL-15 is covalently linked to the IL15Ralpha dimerizing domain via a Gly-Ser linker.

14. The composition of claim 10 or 11, wherein the cytokine is IL-2, wherein the IL-2 comprises the sequence of SEQ ID NO: 2270 or SEQ ID NO: 2191.30 05 2515. The composition of claim 10 or 11, wherein the cytokine is IL-21, wherein the IL-21comprises a sequence having at least 95% sequence identity to the sequence of SEQ ID NO: 2193.

16. The composition of any one of claims 1-15, wherein the molecule further comprises a tumor-targeting moiety.

17. The composition of any one of claims 1-16, wherein the molecule comprises at least twonon-contiguous polypeptide chains;wherein the at least two non-contiguous polypeptide chains comprise a first polypeptide chain and a second polypeptide chain;wherein the first polypeptide chain comprises a first Fc region, and the second polypeptide chain comprises a second Fc region; andwherein the first Fc region and the second Fc region comprise an Fc interface with a knob-in-a hole.

18. The composition of claim 17, wherein:(1) the first Fc region and the second Fc region each comprises an Asn297Ala mutation according to EU Numbering;(2) (i) the first Fc region and the second Fc region each comprises a sequence having at least 90% sequence identity to the sequence of SEQ ID NO: 41, the sequence of SEQ ID NO: 42, or the sequence of SEQ ID NO: 3280; or(ii) (a) the first Fc region comprises a sequence having at least 90% sequence identity to the sequence of SEQ ID NO: 42, with a proviso that the first Fc region comprises Y349C, T366S, L368A, and Y407V mutations according to EU Numbering; and (b) the second Fc region comprises a sequence having at least 90% sequence identity to the sequence of SEQ ID NO: 3280, with a proviso that the second Fc region comprises S354C and T366W mutations according to EU Numbering;(iii) the first Fc region comprises Y349C, T366S, L368A, and Y407V mutations according to EU Numbering, and the second Fc region comprises S354C and T366W mutations according to EU Numbering; or(3) any combination thereof.

19. A recombinant polynucleotide comprising a sequence encoding the molecule of the composition of any one of claims 1-18.30 05 2520. A method of making the molecule of the composition of any one of claims 1-18 comprising culturing a host cell comprising the recombinant polynucleotide of claim 19 under conditions suitable for gene expression and / or homo- or heterodimerization.

21. A pharmaceutical composition comprising the composition of any one of claims 1 -18 for use in treating cancer in a subject in need thereof, wherein the pharmaceutical composition is formulated for administrating a therapeutically effective amount of the composition to the subject, optionally, wherein the subject is human.

22. The pharmaceutical composition of claim 21, wherein the cancer is a solid tumor, a hematological cancer, or a metastatic cancer, optionally, wherein:(i) the cancer is a solid tumor selected from the group consisting of melanoma, pancreatic cancer, breast cancer, colorectal cancer, lung cancer, skin cancer, ovarian cancer, and liver cancer, or(ii) the cancer is a hematological cancer, and the hematological cancer comprises a B-cell malignancy or a T cell malignancy.

23. The composition of any one of claims 1-18 for use in expanding an immune cell population, wherein the composition is formulated for contacting with the immune cell population, and wherein the composition is formulated for the expansion in vivo or ex vivo.

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